PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 31174126-7 2019 Strong dependence on nitric oxide (NO) concentration is found for both observed and modeled HO2 concentrations, with the modeled HO2 decreasing more rapidly than observed HO2, leading to severe HO2 underestimation at higher NO concentrations. Nitric Oxide 21-33 heme oxygenase 2 Homo sapiens 92-95 31575168-8 2019 Using the overlapping qQ3(N = 4-9) transitions of HO2, we estimate limits of detection of 3.1 x 108 cm-3 based on traditional (absorption) CRDS methods and 6.7 x 107 cm-3 using FR-CRDS detection, where each point of the spectrum was acquired during 2 s. In addition, Verdet constants for pertinent carrier (He, Ar) and bulk (N2, O2) gases were recorded in this spectral region for the first time. Nitrogen 325-327 heme oxygenase 2 Homo sapiens 50-53 31174126-7 2019 Strong dependence on nitric oxide (NO) concentration is found for both observed and modeled HO2 concentrations, with the modeled HO2 decreasing more rapidly than observed HO2, leading to severe HO2 underestimation at higher NO concentrations. Nitric Oxide 21-33 heme oxygenase 2 Homo sapiens 129-132 31174126-7 2019 Strong dependence on nitric oxide (NO) concentration is found for both observed and modeled HO2 concentrations, with the modeled HO2 decreasing more rapidly than observed HO2, leading to severe HO2 underestimation at higher NO concentrations. Nitric Oxide 21-33 heme oxygenase 2 Homo sapiens 129-132 31174126-7 2019 Strong dependence on nitric oxide (NO) concentration is found for both observed and modeled HO2 concentrations, with the modeled HO2 decreasing more rapidly than observed HO2, leading to severe HO2 underestimation at higher NO concentrations. Nitric Oxide 21-33 heme oxygenase 2 Homo sapiens 129-132 31132696-4 2019 We conducted a theoretical analysis of the roles of several key factors or parameters in determining gammaHO2 on a sphere droplet with adjustable Cu2+ ion concentration including alphaHO2, aqueous-phase acidity, the first-order loss-rate constant KI value, and the aqueous phase production of HO2. cupric ion 146-150 heme oxygenase 2 Homo sapiens 106-109 31141180-9 2019 These results demonstrated that 5-ALA/SFC treatment ameliorated binge alcohol exposure liver injury in a rat model of HIV-infected patients by reducing macrophage activation and expression of inflammatory cytokines/chemokines, and by inducing HO-1, HO-2, and Sirt1 expression. 5-amino levulinic acid 32-37 heme oxygenase 2 Homo sapiens 249-253 31355843-7 2019 The investigations of the subsequent oxidation processes of the alkyl radical CH3OC(CH3)2CH2C HOH indicated that CH3OC(CH3)2CH2CHO was the most favorable product by eliminating an HO2 radical. alkyl radical ch3oc(ch3)2ch2c hoh 64-97 heme oxygenase 2 Homo sapiens 180-183 31355843-7 2019 The investigations of the subsequent oxidation processes of the alkyl radical CH3OC(CH3)2CH2C HOH indicated that CH3OC(CH3)2CH2CHO was the most favorable product by eliminating an HO2 radical. ch3oc(ch3)2ch2cho 113-130 heme oxygenase 2 Homo sapiens 180-183 31141180-9 2019 These results demonstrated that 5-ALA/SFC treatment ameliorated binge alcohol exposure liver injury in a rat model of HIV-infected patients by reducing macrophage activation and expression of inflammatory cytokines/chemokines, and by inducing HO-1, HO-2, and Sirt1 expression. SFC 38-41 heme oxygenase 2 Homo sapiens 249-253 30942073-12 2019 Hydrogen-bonded adducts of HO2 with the precursors, HO2 CH3OH and HO2 CH3CHO, played a role at lower temperatures; as part of this work, rate enhancements of the HO2 self-reaction due to reactions of the adducts with HO2 were also measured. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 52-55 31276405-5 2019 A distinctive catalytic pathway involving HO2 formation by the activation of H2O2 is found, which gets rid of the restriction of HO2- as the essential initiator in the conventional peroxone reaction. Hydrogen Peroxide 78-82 heme oxygenase 2 Homo sapiens 42-45 31276405-5 2019 A distinctive catalytic pathway involving HO2 formation by the activation of H2O2 is found, which gets rid of the restriction of HO2- as the essential initiator in the conventional peroxone reaction. Hydrogen Peroxide 78-82 heme oxygenase 2 Homo sapiens 130-133 31276405-5 2019 A distinctive catalytic pathway involving HO2 formation by the activation of H2O2 is found, which gets rid of the restriction of HO2- as the essential initiator in the conventional peroxone reaction. peroxone 182-190 heme oxygenase 2 Homo sapiens 42-45 31276405-5 2019 A distinctive catalytic pathway involving HO2 formation by the activation of H2O2 is found, which gets rid of the restriction of HO2- as the essential initiator in the conventional peroxone reaction. peroxone 182-190 heme oxygenase 2 Homo sapiens 130-133 30944174-4 2019 Outside their catalytic cores are two regions unique to HO2: a 20-amino acid-long N-terminal extension and a C-terminal domain containing two heme regulatory motifs (HRMs) that bind heme independently of the core. Heme 142-146 heme oxygenase 2 Homo sapiens 56-59 30944174-4 2019 Outside their catalytic cores are two regions unique to HO2: a 20-amino acid-long N-terminal extension and a C-terminal domain containing two heme regulatory motifs (HRMs) that bind heme independently of the core. Heme 182-186 heme oxygenase 2 Homo sapiens 56-59 30944174-7 2019 Our results reveal that heme binding to the catalytic cores of HO1 and HO2 causes similar dynamic and structural changes in regions (proximal, distal, and A6 helices) within and linked to the heme pocket. Heme 24-28 heme oxygenase 2 Homo sapiens 71-74 30944174-7 2019 Our results reveal that heme binding to the catalytic cores of HO1 and HO2 causes similar dynamic and structural changes in regions (proximal, distal, and A6 helices) within and linked to the heme pocket. Heme 192-196 heme oxygenase 2 Homo sapiens 71-74 30944174-8 2019 We observed that full-length HO2 is more dynamic than truncated forms lacking the membrane-anchoring region, despite sharing the same steady-state activity and heme-binding properties. Heme 160-164 heme oxygenase 2 Homo sapiens 29-32 30942073-4 2019 HO2 and CH3C(O)O2 were formed by Cl-atom reactions with CH3OH and CH3CHO, respectively. Methanol 56-61 heme oxygenase 2 Homo sapiens 0-3 30942073-4 2019 HO2 and CH3C(O)O2 were formed by Cl-atom reactions with CH3OH and CH3CHO, respectively. Acetaldehyde 66-72 heme oxygenase 2 Homo sapiens 0-3 31161168-1 2019 The reaction OH + HO2 H2O + O2 is of great significance in interstellar media, the atmosphere, and combustion. Water 23-26 heme oxygenase 2 Homo sapiens 18-21 31197487-0 2019 A computational study on the characteristics of open-shell H-bonding interaction between carbamic acid (NH2COOH) and HO2, HOS or HSO radicals. carbamic acid 89-102 heme oxygenase 2 Homo sapiens 117-120 31197487-0 2019 A computational study on the characteristics of open-shell H-bonding interaction between carbamic acid (NH2COOH) and HO2, HOS or HSO radicals. nh2cooh 104-111 heme oxygenase 2 Homo sapiens 117-120 31197487-1 2019 Quantum chemical computations were applied to investigate the characteristics of open-shell hydrogen-bonding interactions in the complexes of carbamic acid (NH2COOH, CA) with HO2, HOS and HSO radicals. Hydrogen 92-100 heme oxygenase 2 Homo sapiens 175-178 31197487-1 2019 Quantum chemical computations were applied to investigate the characteristics of open-shell hydrogen-bonding interactions in the complexes of carbamic acid (NH2COOH, CA) with HO2, HOS and HSO radicals. carbamic acid 142-155 heme oxygenase 2 Homo sapiens 175-178 31197487-1 2019 Quantum chemical computations were applied to investigate the characteristics of open-shell hydrogen-bonding interactions in the complexes of carbamic acid (NH2COOH, CA) with HO2, HOS and HSO radicals. nh2cooh 157-164 heme oxygenase 2 Homo sapiens 175-178 31197487-8 2019 Graphical abstract Open-shell H-bondinginteraction between carbamic acid (NH2COOH) and HO2, HOS or HSOradicals. carbamic acid 59-72 heme oxygenase 2 Homo sapiens 87-90 31197487-8 2019 Graphical abstract Open-shell H-bondinginteraction between carbamic acid (NH2COOH) and HO2, HOS or HSOradicals. nh2cooh 74-81 heme oxygenase 2 Homo sapiens 87-90 30990703-4 2019 The RPMD rate coefficients for H + H2O2 OH + H2O are larger than H + H2O2 H2 + HO2, but at very low temperatures below the room temperature, the H2 + HO2 channel becomes dominant due to significant quantum tunneling effects in the H atom transfer process. Hydrogen Peroxide 35-39 heme oxygenase 2 Homo sapiens 154-157 30990703-4 2019 The RPMD rate coefficients for H + H2O2 OH + H2O are larger than H + H2O2 H2 + HO2, but at very low temperatures below the room temperature, the H2 + HO2 channel becomes dominant due to significant quantum tunneling effects in the H atom transfer process. Water 35-38 heme oxygenase 2 Homo sapiens 154-157 30990703-4 2019 The RPMD rate coefficients for H + H2O2 OH + H2O are larger than H + H2O2 H2 + HO2, but at very low temperatures below the room temperature, the H2 + HO2 channel becomes dominant due to significant quantum tunneling effects in the H atom transfer process. Hydrogen Peroxide 71-75 heme oxygenase 2 Homo sapiens 154-157 30990703-4 2019 The RPMD rate coefficients for H + H2O2 OH + H2O are larger than H + H2O2 H2 + HO2, but at very low temperatures below the room temperature, the H2 + HO2 channel becomes dominant due to significant quantum tunneling effects in the H atom transfer process. Hydrogen 35-37 heme oxygenase 2 Homo sapiens 154-157 30942073-12 2019 Hydrogen-bonded adducts of HO2 with the precursors, HO2 CH3OH and HO2 CH3CHO, played a role at lower temperatures; as part of this work, rate enhancements of the HO2 self-reaction due to reactions of the adducts with HO2 were also measured. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 27-30 30942073-12 2019 Hydrogen-bonded adducts of HO2 with the precursors, HO2 CH3OH and HO2 CH3CHO, played a role at lower temperatures; as part of this work, rate enhancements of the HO2 self-reaction due to reactions of the adducts with HO2 were also measured. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 52-55 30942073-12 2019 Hydrogen-bonded adducts of HO2 with the precursors, HO2 CH3OH and HO2 CH3CHO, played a role at lower temperatures; as part of this work, rate enhancements of the HO2 self-reaction due to reactions of the adducts with HO2 were also measured. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 52-55 30942073-12 2019 Hydrogen-bonded adducts of HO2 with the precursors, HO2 CH3OH and HO2 CH3CHO, played a role at lower temperatures; as part of this work, rate enhancements of the HO2 self-reaction due to reactions of the adducts with HO2 were also measured. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 52-55 30876351-14 2019 A new aerobic reaction cycle is hypothesized, wherein dissolved dioxygen captures radiolytic H or eaq -, enters HO2 /O2 -, reductively quenches cysteine thiyl radicals, and cycles back to O2. Oxygen 64-72 heme oxygenase 2 Homo sapiens 113-116 30802768-6 2019 The formed MoOCo further leads to a distribution of orientations of the electrons around the metal centers due to the different electronegativity of Mo and Co. During the reaction, the dissolved O2 is efficiently reduced to HO2/O2- around the electron-rich Mo center, and HO2/O2- is further reduced to H2O2 around the Co center. Oxygen 195-197 heme oxygenase 2 Homo sapiens 224-227 30802768-6 2019 The formed MoOCo further leads to a distribution of orientations of the electrons around the metal centers due to the different electronegativity of Mo and Co. During the reaction, the dissolved O2 is efficiently reduced to HO2/O2- around the electron-rich Mo center, and HO2/O2- is further reduced to H2O2 around the Co center. Oxygen 195-197 heme oxygenase 2 Homo sapiens 272-275 30802768-6 2019 The formed MoOCo further leads to a distribution of orientations of the electrons around the metal centers due to the different electronegativity of Mo and Co. During the reaction, the dissolved O2 is efficiently reduced to HO2/O2- around the electron-rich Mo center, and HO2/O2- is further reduced to H2O2 around the Co center. Oxygen 225-227 heme oxygenase 2 Homo sapiens 272-275 30802768-6 2019 The formed MoOCo further leads to a distribution of orientations of the electrons around the metal centers due to the different electronegativity of Mo and Co. During the reaction, the dissolved O2 is efficiently reduced to HO2/O2- around the electron-rich Mo center, and HO2/O2- is further reduced to H2O2 around the Co center. Oxygen 225-227 heme oxygenase 2 Homo sapiens 272-275 30802768-6 2019 The formed MoOCo further leads to a distribution of orientations of the electrons around the metal centers due to the different electronegativity of Mo and Co. During the reaction, the dissolved O2 is efficiently reduced to HO2/O2- around the electron-rich Mo center, and HO2/O2- is further reduced to H2O2 around the Co center. Hydrogen Peroxide 302-306 heme oxygenase 2 Homo sapiens 224-227 30802768-6 2019 The formed MoOCo further leads to a distribution of orientations of the electrons around the metal centers due to the different electronegativity of Mo and Co. During the reaction, the dissolved O2 is efficiently reduced to HO2/O2- around the electron-rich Mo center, and HO2/O2- is further reduced to H2O2 around the Co center. Hydrogen Peroxide 302-306 heme oxygenase 2 Homo sapiens 272-275 30938991-0 2019 Ho2O@C74: Ho2O Cluster Expands within a Small Non-IPR Fullerene Cage of C2(13333)-C74. Fullerenes 54-63 heme oxygenase 2 Homo sapiens 0-3 29235938-6 2019 In the short initial stage, the utilization efficiency of H2O2 was high, because the generation rate of OH was much higher than that of HO2 . Hydrogen Peroxide 58-62 heme oxygenase 2 Homo sapiens 137-140 29235938-9 2019 Most of the OH radicals were consumed via the rapid useless reaction between OH and HO2 in this stage, resulting in the serious useless consumption of H2O2. oh radicals 13-24 heme oxygenase 2 Homo sapiens 86-89 29235938-9 2019 Most of the OH radicals were consumed via the rapid useless reaction between OH and HO2 in this stage, resulting in the serious useless consumption of H2O2. Hydrogen Peroxide 154-158 heme oxygenase 2 Homo sapiens 86-89 29235938-10 2019 It is a feasible method to improve the utilization efficiency of H2O2 by adding suitable additives into the Fe2+/H2O2 system to weaken the useless reaction between OH and HO2 . Hydrogen Peroxide 65-69 heme oxygenase 2 Homo sapiens 172-175 29235938-10 2019 It is a feasible method to improve the utilization efficiency of H2O2 by adding suitable additives into the Fe2+/H2O2 system to weaken the useless reaction between OH and HO2 . ammonium ferrous sulfate 108-112 heme oxygenase 2 Homo sapiens 172-175 29235938-10 2019 It is a feasible method to improve the utilization efficiency of H2O2 by adding suitable additives into the Fe2+/H2O2 system to weaken the useless reaction between OH and HO2 . Hydrogen Peroxide 113-117 heme oxygenase 2 Homo sapiens 172-175 30876351-14 2019 A new aerobic reaction cycle is hypothesized, wherein dissolved dioxygen captures radiolytic H or eaq -, enters HO2 /O2 -, reductively quenches cysteine thiyl radicals, and cycles back to O2. cysteine thiyl radicals 147-170 heme oxygenase 2 Homo sapiens 113-116 30876351-14 2019 A new aerobic reaction cycle is hypothesized, wherein dissolved dioxygen captures radiolytic H or eaq -, enters HO2 /O2 -, reductively quenches cysteine thiyl radicals, and cycles back to O2. Oxygen 119-121 heme oxygenase 2 Homo sapiens 113-116 30620599-0 2019 Chemical Kinetics of H-Atom Abstraction from Ethanol by HO2: Implication for Combustion Modeling. Ethanol 45-52 heme oxygenase 2 Homo sapiens 56-59 30688319-4 2019 In this work, we find that carbon plays an important synergistic role in improving the performance of La1-xSrxCoO3-delta (0 <= x <= 1) electrocatalysts through the activation of O2 and spillover of radical oxygen intermediates, HO2- and O2-, which is further reduced through chemical decomposition of HO2- on the perovskite surface. Carbon 27-33 heme oxygenase 2 Homo sapiens 234-237 30688319-4 2019 In this work, we find that carbon plays an important synergistic role in improving the performance of La1-xSrxCoO3-delta (0 <= x <= 1) electrocatalysts through the activation of O2 and spillover of radical oxygen intermediates, HO2- and O2-, which is further reduced through chemical decomposition of HO2- on the perovskite surface. Carbon 27-33 heme oxygenase 2 Homo sapiens 307-310 30688319-4 2019 In this work, we find that carbon plays an important synergistic role in improving the performance of La1-xSrxCoO3-delta (0 <= x <= 1) electrocatalysts through the activation of O2 and spillover of radical oxygen intermediates, HO2- and O2-, which is further reduced through chemical decomposition of HO2- on the perovskite surface. Oxygen 184-186 heme oxygenase 2 Homo sapiens 234-237 30688319-4 2019 In this work, we find that carbon plays an important synergistic role in improving the performance of La1-xSrxCoO3-delta (0 <= x <= 1) electrocatalysts through the activation of O2 and spillover of radical oxygen intermediates, HO2- and O2-, which is further reduced through chemical decomposition of HO2- on the perovskite surface. Oxygen 184-186 heme oxygenase 2 Homo sapiens 307-310 30453228-7 2019 It indicated that the main oxidative species in the photocatalytic degradation process were holes and hydro oxygen radicals (e.g. HO2 and H2O2). hydro oxygen radicals 102-123 heme oxygenase 2 Homo sapiens 130-133 30620599-3 2019 The reaction mechanism of ethanol + HO2 is a well-known crucial reaction class in terms of predicting the reactivity of ethanol as well as ethylene formation under engine-relevant conditions. Ethanol 26-33 heme oxygenase 2 Homo sapiens 36-39 30620599-3 2019 The reaction mechanism of ethanol + HO2 is a well-known crucial reaction class in terms of predicting the reactivity of ethanol as well as ethylene formation under engine-relevant conditions. Ethanol 120-127 heme oxygenase 2 Homo sapiens 36-39 30620599-3 2019 The reaction mechanism of ethanol + HO2 is a well-known crucial reaction class in terms of predicting the reactivity of ethanol as well as ethylene formation under engine-relevant conditions. ethylene 139-147 heme oxygenase 2 Homo sapiens 36-39 30620599-4 2019 However, the kinetic parameters of the reactions are basically extrapolated by analogy to the n-butanol + HO2 system calculated by Zhou et al. 1-Butanol 94-103 heme oxygenase 2 Homo sapiens 106-109 30620599-11 2019 In this study, thermal rate coefficients of H-atom abstraction reactions for the ethanol + HO2 system were determined by using both conventional transition-state theory and canonical variational transition-state theory, with the potential energy surface evaluated at the CCSD(T)/cc-pVTZ//M06-2x/def-TZVP level. Ethanol 81-88 heme oxygenase 2 Homo sapiens 91-94 30620599-11 2019 In this study, thermal rate coefficients of H-atom abstraction reactions for the ethanol + HO2 system were determined by using both conventional transition-state theory and canonical variational transition-state theory, with the potential energy surface evaluated at the CCSD(T)/cc-pVTZ//M06-2x/def-TZVP level. tzvp 299-303 heme oxygenase 2 Homo sapiens 91-94 30620599-15 2019 Similar to the n-butanol + HO2 system, the title system is dominated by alpha-site H-atom abstraction, but the rate coefficients of the three channels are slightly slower than that of the n-butanol + HO2 system. 1-Butanol 15-24 heme oxygenase 2 Homo sapiens 27-30 30620599-15 2019 Similar to the n-butanol + HO2 system, the title system is dominated by alpha-site H-atom abstraction, but the rate coefficients of the three channels are slightly slower than that of the n-butanol + HO2 system. 1-Butanol 15-24 heme oxygenase 2 Homo sapiens 200-203 30620599-15 2019 Similar to the n-butanol + HO2 system, the title system is dominated by alpha-site H-atom abstraction, but the rate coefficients of the three channels are slightly slower than that of the n-butanol + HO2 system. 1-Butanol 188-197 heme oxygenase 2 Homo sapiens 27-30 30620599-15 2019 Similar to the n-butanol + HO2 system, the title system is dominated by alpha-site H-atom abstraction, but the rate coefficients of the three channels are slightly slower than that of the n-butanol + HO2 system. 1-Butanol 188-197 heme oxygenase 2 Homo sapiens 200-203 30511221-10 2019 The reaction of alkyl peroxy radical intermediate with atmospheric oxidants, HO2, NO, and NO2 is also studied. alkyl peroxy radical 16-36 heme oxygenase 2 Homo sapiens 77-80 31459335-6 2019 On the other hand, as for the reaction of the anion of H2O2 (HO2 -), the nucleophilic addition of HO2 - to TCDF can also occur besides the nucleophilic aromatic substitution reaction mentioned above, resulting in the dissociation of the C-O bond of TCDF. Hydrogen Peroxide 55-59 heme oxygenase 2 Homo sapiens 61-64 30656304-10 2019 For the largest loadings of dust in the troposphere, the rate of this novel heterogeneous production mechanism begins to approach that of HO2 production from the gas-phase reaction of OH with CO in unpolluted regions. Carbon Monoxide 192-194 heme oxygenase 2 Homo sapiens 138-141 30656304-0 2019 Production of HO2 and OH radicals from near-UV irradiated airborne TiO2 nanoparticles. titanium dioxide 67-71 heme oxygenase 2 Homo sapiens 14-17 30656304-1 2019 The production of gas-phase hydroperoxyl radicals, HO2, is observed directly from sub-micron airborne TiO2 nanoparticles irradiated by 300-400 nm radiation. hydroperoxyl radicals 28-49 heme oxygenase 2 Homo sapiens 51-54 30656304-1 2019 The production of gas-phase hydroperoxyl radicals, HO2, is observed directly from sub-micron airborne TiO2 nanoparticles irradiated by 300-400 nm radiation. titanium dioxide 102-106 heme oxygenase 2 Homo sapiens 51-54 30656304-2 2019 The rate of HO2 production as a function of O2 pressure follows Langmuir isotherm behaviour suggesting O2 is involved in the production of HO2 following its adsorption onto the surface of the TiO2 aerosol. Oxygen 13-15 heme oxygenase 2 Homo sapiens 139-142 30656304-2 2019 The rate of HO2 production as a function of O2 pressure follows Langmuir isotherm behaviour suggesting O2 is involved in the production of HO2 following its adsorption onto the surface of the TiO2 aerosol. Oxygen 44-46 heme oxygenase 2 Homo sapiens 12-15 30656304-2 2019 The rate of HO2 production as a function of O2 pressure follows Langmuir isotherm behaviour suggesting O2 is involved in the production of HO2 following its adsorption onto the surface of the TiO2 aerosol. Oxygen 44-46 heme oxygenase 2 Homo sapiens 139-142 30656304-2 2019 The rate of HO2 production as a function of O2 pressure follows Langmuir isotherm behaviour suggesting O2 is involved in the production of HO2 following its adsorption onto the surface of the TiO2 aerosol. titanium dioxide 192-196 heme oxygenase 2 Homo sapiens 12-15 30656304-2 2019 The rate of HO2 production as a function of O2 pressure follows Langmuir isotherm behaviour suggesting O2 is involved in the production of HO2 following its adsorption onto the surface of the TiO2 aerosol. titanium dioxide 192-196 heme oxygenase 2 Homo sapiens 139-142 30656304-4 2019 The rate of HO2 production decreased significantly over the range of relative humidities between 8.7 and 36.9%, suggesting competitive adsorption of water vapour inhibits HO2 production. Water 149-154 heme oxygenase 2 Homo sapiens 12-15 30656304-4 2019 The rate of HO2 production decreased significantly over the range of relative humidities between 8.7 and 36.9%, suggesting competitive adsorption of water vapour inhibits HO2 production. Water 149-154 heme oxygenase 2 Homo sapiens 171-174 30656304-6 2019 The increased coverage of H2O onto the TiO2 aerosol surface may inhibit HO2 production by decreasing the effective surface area of the TiO2 particle and lowering the binding energy of O2 on the aerosol surface, hence shortening its desorption lifetime. Water 26-29 heme oxygenase 2 Homo sapiens 72-75 30656304-6 2019 The increased coverage of H2O onto the TiO2 aerosol surface may inhibit HO2 production by decreasing the effective surface area of the TiO2 particle and lowering the binding energy of O2 on the aerosol surface, hence shortening its desorption lifetime. titanium dioxide 39-43 heme oxygenase 2 Homo sapiens 72-75 30656304-6 2019 The increased coverage of H2O onto the TiO2 aerosol surface may inhibit HO2 production by decreasing the effective surface area of the TiO2 particle and lowering the binding energy of O2 on the aerosol surface, hence shortening its desorption lifetime. titanium dioxide 135-139 heme oxygenase 2 Homo sapiens 72-75 30656304-6 2019 The increased coverage of H2O onto the TiO2 aerosol surface may inhibit HO2 production by decreasing the effective surface area of the TiO2 particle and lowering the binding energy of O2 on the aerosol surface, hence shortening its desorption lifetime. Oxygen 41-43 heme oxygenase 2 Homo sapiens 72-75 30656304-7 2019 The maximum yield (i.e. when [O2] is projected to atmospherically relevant levels) for production of gas-phase HO2, normalised for surface area and light intensity, was found to be at a RH of 8.7% for the 80% anatase and 20% rutile formulation of TiO2 used here. Oxygen 30-32 heme oxygenase 2 Homo sapiens 111-114 30656304-7 2019 The maximum yield (i.e. when [O2] is projected to atmospherically relevant levels) for production of gas-phase HO2, normalised for surface area and light intensity, was found to be at a RH of 8.7% for the 80% anatase and 20% rutile formulation of TiO2 used here. titanium dioxide 247-251 heme oxygenase 2 Homo sapiens 111-114 30656304-9 2019 Using this value, the rate of production of HO2 from TiO2 surfaces under atmospheric conditions was estimated to be in the range 5 x 104-1 x 106 molecule cm-3 s-1 using observed surface areas of mineral dust at Cape Verde, and assuming a TiO2 fraction of 4.5%. titanium dioxide 53-57 heme oxygenase 2 Homo sapiens 44-47 30656304-9 2019 Using this value, the rate of production of HO2 from TiO2 surfaces under atmospheric conditions was estimated to be in the range 5 x 104-1 x 106 molecule cm-3 s-1 using observed surface areas of mineral dust at Cape Verde, and assuming a TiO2 fraction of 4.5%. titanium dioxide 238-242 heme oxygenase 2 Homo sapiens 44-47 30723777-5 2019 Results: We found that the expression levels of the rate-limiting heme synthetic enzyme ALAS1 and heme degradation enzyme HO-2 are selectively decreased in AD patients and mice. Heme 66-70 heme oxygenase 2 Homo sapiens 122-126 30723777-7 2019 Discussion: Our data show that lowered heme metabolism, particularly the decreased levels of heme degradation and HO-2, is likely a very early event in AD pathogenesis. Heme 39-43 heme oxygenase 2 Homo sapiens 114-118 31459335-6 2019 On the other hand, as for the reaction of the anion of H2O2 (HO2 -), the nucleophilic addition of HO2 - to TCDF can also occur besides the nucleophilic aromatic substitution reaction mentioned above, resulting in the dissociation of the C-O bond of TCDF. Hydrogen Peroxide 55-59 heme oxygenase 2 Homo sapiens 98-101 31459335-6 2019 On the other hand, as for the reaction of the anion of H2O2 (HO2 -), the nucleophilic addition of HO2 - to TCDF can also occur besides the nucleophilic aromatic substitution reaction mentioned above, resulting in the dissociation of the C-O bond of TCDF. 2,3,7,8-tetrachlorodibenzofuran 107-111 heme oxygenase 2 Homo sapiens 61-64 31459335-6 2019 On the other hand, as for the reaction of the anion of H2O2 (HO2 -), the nucleophilic addition of HO2 - to TCDF can also occur besides the nucleophilic aromatic substitution reaction mentioned above, resulting in the dissociation of the C-O bond of TCDF. 2,3,7,8-tetrachlorodibenzofuran 107-111 heme oxygenase 2 Homo sapiens 98-101 31459335-6 2019 On the other hand, as for the reaction of the anion of H2O2 (HO2 -), the nucleophilic addition of HO2 - to TCDF can also occur besides the nucleophilic aromatic substitution reaction mentioned above, resulting in the dissociation of the C-O bond of TCDF. 2,3,7,8-tetrachlorodibenzofuran 249-253 heme oxygenase 2 Homo sapiens 61-64 31459335-6 2019 On the other hand, as for the reaction of the anion of H2O2 (HO2 -), the nucleophilic addition of HO2 - to TCDF can also occur besides the nucleophilic aromatic substitution reaction mentioned above, resulting in the dissociation of the C-O bond of TCDF. 2,3,7,8-tetrachlorodibenzofuran 249-253 heme oxygenase 2 Homo sapiens 98-101 30484312-2 2019 They are photoreactive and can act as an important source of reactive oxygen species ( OH, H2O2 and HO2 ) in tropospheric aqueous phases. Reactive Oxygen Species 61-84 heme oxygenase 2 Homo sapiens 100-103 30553057-1 2019 Carbon monoxide (CO) is an anti-inflammatory gaseous molecule produced endogenously by heme oxygenases (HOs) HO-1 and HO-2. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 109-122 30467745-1 2019 Using quantum chemistry methods, mechanisms and products of the CHBr2O2 + HO2 reaction in the atmosphere were investigated theoretically. chbr2o2 64-71 heme oxygenase 2 Homo sapiens 74-77 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. cbr2o 6-11 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. cbr2o2 210-216 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. Hydrogen Peroxide 219-223 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. cbr2o 210-215 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. ho3h 233-237 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. Formaldehyde 239-243 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. ho3br 246-251 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. chbro 253-258 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. Bromine 7-9 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. chbr2oh 275-282 heme oxygenase 2 Homo sapiens 19-22 30467745-3 2019 While CBr2O + OH + HO2 produced on the singlet PES is subdominant to the overall reaction under the typical atmospheric condition below 300 K. Due to higher energy barriers surmounted, other products including CBr2O2 + H2O2, CBr2O + HO3H, CH2O + HO3Br, CHBrO + HO3 + Br, and CHBr2OH + O3 make minor contributions to the overall reaction. Ozone 234-236 heme oxygenase 2 Homo sapiens 19-22 30467745-5 2019 The substitution effect of alkyl group and halogens plays negligible roles to the dominant products in the RO2 + HO2 (X = H, CH3, CH2OH, CH2F, CH2Cl, CH2Br, CH2Cl, and CH2Br) reactions in the atmosphere. ro2 107-110 heme oxygenase 2 Homo sapiens 113-116 30553057-1 2019 Carbon monoxide (CO) is an anti-inflammatory gaseous molecule produced endogenously by heme oxygenases (HOs) HO-1 and HO-2. Carbon Monoxide 17-19 heme oxygenase 2 Homo sapiens 109-122 30243703-5 2018 Generally, the main radical species detected in hair oxidative coloring or bleaching processes, were hydroperoxyl/superoxide radicals HO2 /O2.-, amino radicals NH2 and hydroxyl radicals OH. hydroperoxyl/superoxide radicals 101-133 heme oxygenase 2 Homo sapiens 134-137 30960021-6 2018 Results showed that the reactive species of OH , HO2 and H3O+ were produced during the plasma discharge of water. Water 108-113 heme oxygenase 2 Homo sapiens 49-52 28990415-6 2018 Because the cysteines must be in the reduced, dithiol form to act as a heme axial ligand, heme binds at these sites in a redox-regulated manner, as demonstrated for heme oxygenase-2 (HO2) and Rev-erbbeta. Cysteine 12-21 heme oxygenase 2 Homo sapiens 165-181 28990415-6 2018 Because the cysteines must be in the reduced, dithiol form to act as a heme axial ligand, heme binds at these sites in a redox-regulated manner, as demonstrated for heme oxygenase-2 (HO2) and Rev-erbbeta. Cysteine 12-21 heme oxygenase 2 Homo sapiens 183-186 28990415-6 2018 Because the cysteines must be in the reduced, dithiol form to act as a heme axial ligand, heme binds at these sites in a redox-regulated manner, as demonstrated for heme oxygenase-2 (HO2) and Rev-erbbeta. dithiol 46-53 heme oxygenase 2 Homo sapiens 183-186 28990415-6 2018 Because the cysteines must be in the reduced, dithiol form to act as a heme axial ligand, heme binds at these sites in a redox-regulated manner, as demonstrated for heme oxygenase-2 (HO2) and Rev-erbbeta. Heme 71-75 heme oxygenase 2 Homo sapiens 165-181 28990415-6 2018 Because the cysteines must be in the reduced, dithiol form to act as a heme axial ligand, heme binds at these sites in a redox-regulated manner, as demonstrated for heme oxygenase-2 (HO2) and Rev-erbbeta. Heme 71-75 heme oxygenase 2 Homo sapiens 183-186 28990415-6 2018 Because the cysteines must be in the reduced, dithiol form to act as a heme axial ligand, heme binds at these sites in a redox-regulated manner, as demonstrated for heme oxygenase-2 (HO2) and Rev-erbbeta. Heme 90-94 heme oxygenase 2 Homo sapiens 165-181 28990415-6 2018 Because the cysteines must be in the reduced, dithiol form to act as a heme axial ligand, heme binds at these sites in a redox-regulated manner, as demonstrated for heme oxygenase-2 (HO2) and Rev-erbbeta. Heme 90-94 heme oxygenase 2 Homo sapiens 183-186 30449100-0 2018 Computational Investigation of RO2 + HO2 and RO2 + RO2 Reactions of Monoterpene Derived First-Generation Peroxy Radicals Leading to Radical Recycling. ro2 31-34 heme oxygenase 2 Homo sapiens 37-40 30376334-5 2018 The dominant products in the presence of O2/NO are epoxide, dialdehyde, alcohol ketone, cyclolactone compounds, and HO2 radicals. Oxygen 41-43 heme oxygenase 2 Homo sapiens 116-119 30449100-3 2018 Under clean (low-NO x) conditions, the main bimolecular sink reactions for RO2 are with the hydroperoxy radical (HO2) and with other RO2 radicals. ro2 75-78 heme oxygenase 2 Homo sapiens 113-116 30449100-3 2018 Under clean (low-NO x) conditions, the main bimolecular sink reactions for RO2 are with the hydroperoxy radical (HO2) and with other RO2 radicals. perhydroxyl radical 92-111 heme oxygenase 2 Homo sapiens 113-116 30449100-4 2018 Especially for small RO2, the RO2 + HO2 reaction mainly leads to closed-shell hydroperoxide products. ro2 21-24 heme oxygenase 2 Homo sapiens 36-39 30449100-4 2018 Especially for small RO2, the RO2 + HO2 reaction mainly leads to closed-shell hydroperoxide products. ro2 30-33 heme oxygenase 2 Homo sapiens 36-39 30449100-4 2018 Especially for small RO2, the RO2 + HO2 reaction mainly leads to closed-shell hydroperoxide products. Hydrogen Peroxide 78-91 heme oxygenase 2 Homo sapiens 36-39 30449100-6 2018 In this work, we present a thermodynamic overview of two such reactions: (a) RO2 + HO2 RO + OH + O2 and (b) R"O2 + RO2 R"O + RO + O2 for selected monoterpene + oxidant derived peroxy radicals. ro2 77-80 heme oxygenase 2 Homo sapiens 83-86 30449100-6 2018 In this work, we present a thermodynamic overview of two such reactions: (a) RO2 + HO2 RO + OH + O2 and (b) R"O2 + RO2 R"O + RO + O2 for selected monoterpene + oxidant derived peroxy radicals. r"o2 110-114 heme oxygenase 2 Homo sapiens 83-86 30449100-6 2018 In this work, we present a thermodynamic overview of two such reactions: (a) RO2 + HO2 RO + OH + O2 and (b) R"O2 + RO2 R"O + RO + O2 for selected monoterpene + oxidant derived peroxy radicals. ro2 117-120 heme oxygenase 2 Homo sapiens 83-86 30449100-6 2018 In this work, we present a thermodynamic overview of two such reactions: (a) RO2 + HO2 RO + OH + O2 and (b) R"O2 + RO2 R"O + RO + O2 for selected monoterpene + oxidant derived peroxy radicals. Oxygen 78-80 heme oxygenase 2 Homo sapiens 83-86 30449100-6 2018 In this work, we present a thermodynamic overview of two such reactions: (a) RO2 + HO2 RO + OH + O2 and (b) R"O2 + RO2 R"O + RO + O2 for selected monoterpene + oxidant derived peroxy radicals. Monoterpenes 150-161 heme oxygenase 2 Homo sapiens 83-86 30449100-6 2018 In this work, we present a thermodynamic overview of two such reactions: (a) RO2 + HO2 RO + OH + O2 and (b) R"O2 + RO2 R"O + RO + O2 for selected monoterpene + oxidant derived peroxy radicals. peroxy radicals 180-195 heme oxygenase 2 Homo sapiens 83-86 30449100-13 2018 Our results indicate that bimolecular reactions of certain complex RO2 may contribute to an increase in radical and oxidant recycling under high HO2 conditions in the atmosphere, which can potentially enhance SOA formation. ro2 67-70 heme oxygenase 2 Homo sapiens 145-148 30409010-0 2018 Rate coefficients of the H + H2O2 H2 + HO2 reaction on an accurate fundamental invariant-neural network potential energy surface. Hydrogen Peroxide 29-33 heme oxygenase 2 Homo sapiens 41-44 30409010-0 2018 Rate coefficients of the H + H2O2 H2 + HO2 reaction on an accurate fundamental invariant-neural network potential energy surface. Hydrogen 29-31 heme oxygenase 2 Homo sapiens 41-44 30409010-1 2018 The rate coefficients of the H + H2O2 H2 + HO2 reaction are calculated using the ring polymer molecular dynamics (RPMD), quasi-classical trajectory (QCT), and canonical variational transition state theory (CVT) with small curvature tunneling (SCT) correction, in conjunction with the recently constructed fundamental invariant-neural network (FI-NN) potential energy surface (PES) [X. Lu et al., Phys. Hydrogen Peroxide 33-37 heme oxygenase 2 Homo sapiens 45-48 30409010-1 2018 The rate coefficients of the H + H2O2 H2 + HO2 reaction are calculated using the ring polymer molecular dynamics (RPMD), quasi-classical trajectory (QCT), and canonical variational transition state theory (CVT) with small curvature tunneling (SCT) correction, in conjunction with the recently constructed fundamental invariant-neural network (FI-NN) potential energy surface (PES) [X. Lu et al., Phys. Polymers 88-95 heme oxygenase 2 Homo sapiens 45-48 30255207-1 2018 The potential energy surface for the first step of the methane oxidation CH4 + O2 CH3 + HO2 was studied using the London-Eyring-Polanyi-Sato equation (LEPS) and the conventional transition-state theory (CTST). Methane 55-62 heme oxygenase 2 Homo sapiens 88-91 30272487-0 2018 Use of quantum-chemical descriptors to analyse reaction rate constants between organic chemicals and superoxide/hydroperoxyl (O2 -/HO2 ). Superoxides 101-111 heme oxygenase 2 Homo sapiens 131-134 30272487-0 2018 Use of quantum-chemical descriptors to analyse reaction rate constants between organic chemicals and superoxide/hydroperoxyl (O2 -/HO2 ). perhydroxyl radical 112-124 heme oxygenase 2 Homo sapiens 131-134 30339546-6 2018 The reactive oxygen radicals identified using electron spin resonance (ESR) spectroscopy revealed that hydroxyl radical was dominant oxidant in UV-Fe2+-Fenton process, while HO2 /O2 - played a more important role in the UV-Cu-Fenton system. reactive oxygen radicals 4-28 heme oxygenase 2 Homo sapiens 174-177 30255207-1 2018 The potential energy surface for the first step of the methane oxidation CH4 + O2 CH3 + HO2 was studied using the London-Eyring-Polanyi-Sato equation (LEPS) and the conventional transition-state theory (CTST). Methane 73-76 heme oxygenase 2 Homo sapiens 88-91 30255207-1 2018 The potential energy surface for the first step of the methane oxidation CH4 + O2 CH3 + HO2 was studied using the London-Eyring-Polanyi-Sato equation (LEPS) and the conventional transition-state theory (CTST). Oxygen 79-81 heme oxygenase 2 Homo sapiens 88-91 30255207-1 2018 The potential energy surface for the first step of the methane oxidation CH4 + O2 CH3 + HO2 was studied using the London-Eyring-Polanyi-Sato equation (LEPS) and the conventional transition-state theory (CTST). methyl radical 82-85 heme oxygenase 2 Homo sapiens 88-91 30255207-1 2018 The potential energy surface for the first step of the methane oxidation CH4 + O2 CH3 + HO2 was studied using the London-Eyring-Polanyi-Sato equation (LEPS) and the conventional transition-state theory (CTST). ctst 203-207 heme oxygenase 2 Homo sapiens 88-91 30168544-1 2018 We report a new full-dimensional potential energy surface (PES) of the H + H2O2 reaction, covering both H2 + HO2 and OH + H2O product channels. Hydrogen Peroxide 75-79 heme oxygenase 2 Homo sapiens 109-112 29892732-1 2018 The hydrogen abstraction reactions of phenyl formate (PF) by different radicals (H/O(3P)/OH/HO2) were theoretically investigated. Hydrogen 4-12 heme oxygenase 2 Homo sapiens 92-95 29892732-1 2018 The hydrogen abstraction reactions of phenyl formate (PF) by different radicals (H/O(3P)/OH/HO2) were theoretically investigated. Benzoic Acid 38-52 heme oxygenase 2 Homo sapiens 92-95 29892732-1 2018 The hydrogen abstraction reactions of phenyl formate (PF) by different radicals (H/O(3P)/OH/HO2) were theoretically investigated. Benzoic Acid 54-56 heme oxygenase 2 Homo sapiens 92-95 29893740-7 2018 In the oxidation stage, Mn(II) promotes the production of HO2 / O2 -, then HO2 / O2 - reacts with Fe(III) to accelerate the formation of Fe(II), and finally accelerates the production of HO . Manganese(2+) 24-30 heme oxygenase 2 Homo sapiens 58-61 29957938-4 2018 Unimolecular reaction of this R-C(OO)(OH)2 radical adduct, occurs via a proton-coupled electron transfer (PCET) mechanism and leads to the formation of an organic acid and a HO2 radical. r-c(oo)(oh)2 radical 30-50 heme oxygenase 2 Homo sapiens 174-177 29957938-4 2018 Unimolecular reaction of this R-C(OO)(OH)2 radical adduct, occurs via a proton-coupled electron transfer (PCET) mechanism and leads to the formation of an organic acid and a HO2 radical. pcet 106-110 heme oxygenase 2 Homo sapiens 174-177 29957938-7 2018 The rate constants for the four diol oxidation reactions were investigated using the MESMER master equation solver kinetics code over the temperature range between 200 and 300 K. The calculations suggest that once formed, gem diol radicals react rapidly with O2 in the atmosphere to produce organic acids and HO2 with an effective gas phase bimolecular rate constant of ~1 x 10-11 cm3/molecule s at 300 K. diol 32-36 heme oxygenase 2 Homo sapiens 309-312 29957938-7 2018 The rate constants for the four diol oxidation reactions were investigated using the MESMER master equation solver kinetics code over the temperature range between 200 and 300 K. The calculations suggest that once formed, gem diol radicals react rapidly with O2 in the atmosphere to produce organic acids and HO2 with an effective gas phase bimolecular rate constant of ~1 x 10-11 cm3/molecule s at 300 K. diol 226-230 heme oxygenase 2 Homo sapiens 309-312 29957938-7 2018 The rate constants for the four diol oxidation reactions were investigated using the MESMER master equation solver kinetics code over the temperature range between 200 and 300 K. The calculations suggest that once formed, gem diol radicals react rapidly with O2 in the atmosphere to produce organic acids and HO2 with an effective gas phase bimolecular rate constant of ~1 x 10-11 cm3/molecule s at 300 K. Oxygen 259-261 heme oxygenase 2 Homo sapiens 309-312 29957938-7 2018 The rate constants for the four diol oxidation reactions were investigated using the MESMER master equation solver kinetics code over the temperature range between 200 and 300 K. The calculations suggest that once formed, gem diol radicals react rapidly with O2 in the atmosphere to produce organic acids and HO2 with an effective gas phase bimolecular rate constant of ~1 x 10-11 cm3/molecule s at 300 K. organic acids 291-304 heme oxygenase 2 Homo sapiens 309-312 29426148-8 2018 The reactions of OH and Cl radicals with HCBD are more important than those of NO3, HO2 and O3 according to the reaction rate branching ratio. cl radicals 24-35 heme oxygenase 2 Homo sapiens 84-87 29426148-8 2018 The reactions of OH and Cl radicals with HCBD are more important than those of NO3, HO2 and O3 according to the reaction rate branching ratio. hexachlorobutadiene 41-45 heme oxygenase 2 Homo sapiens 84-87 29792704-0 2018 Double Hydrogen-Atom Exchange Reactions of HX (X = F, Cl, Br, I) with HO2. Hydrogen 7-15 heme oxygenase 2 Homo sapiens 70-73 29893740-7 2018 In the oxidation stage, Mn(II) promotes the production of HO2 / O2 -, then HO2 / O2 - reacts with Fe(III) to accelerate the formation of Fe(II), and finally accelerates the production of HO . Oxygen 64-66 heme oxygenase 2 Homo sapiens 58-61 29893740-7 2018 In the oxidation stage, Mn(II) promotes the production of HO2 / O2 -, then HO2 / O2 - reacts with Fe(III) to accelerate the formation of Fe(II), and finally accelerates the production of HO . ferric sulfate 98-105 heme oxygenase 2 Homo sapiens 75-78 29893740-7 2018 In the oxidation stage, Mn(II) promotes the production of HO2 / O2 -, then HO2 / O2 - reacts with Fe(III) to accelerate the formation of Fe(II), and finally accelerates the production of HO . ammonium ferrous sulfate 137-143 heme oxygenase 2 Homo sapiens 75-78 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Reactive Oxygen Species 24-27 heme oxygenase 2 Homo sapiens 133-149 28960009-0 2018 Effect of a single water molecule on the HO2 + ClO reaction. Water 19-24 heme oxygenase 2 Homo sapiens 41-44 28960009-1 2018 The catalytic effect of a single water molecule on the HO2 + ClO reaction has been investigated at the CCSD(T)/aug-cc-pVTZ//B3LYP-D3/aug-cc-pVDZ level of theory. Water 33-38 heme oxygenase 2 Homo sapiens 55-58 28960009-2 2018 Four H-abstraction paths and two kinds of products, among which the paths for HOCl + O2 formation are dominant, have been found for the HO2 + ClO reaction without water. Hypochlorous Acid 78-82 heme oxygenase 2 Homo sapiens 136-139 28960009-2 2018 Four H-abstraction paths and two kinds of products, among which the paths for HOCl + O2 formation are dominant, have been found for the HO2 + ClO reaction without water. Oxygen 85-87 heme oxygenase 2 Homo sapiens 136-139 28960009-2 2018 Four H-abstraction paths and two kinds of products, among which the paths for HOCl + O2 formation are dominant, have been found for the HO2 + ClO reaction without water. Water 163-168 heme oxygenase 2 Homo sapiens 136-139 28960009-6 2018 The most favorable paths, reactions between H2OHO2 and ClO, and between ClOH2O and HO2, are 7-10 and 6-9 orders of magnitude slower than the reaction in the absence of water, respectively. Hypochlorous Acid 55-58 heme oxygenase 2 Homo sapiens 47-50 28960009-6 2018 The most favorable paths, reactions between H2OHO2 and ClO, and between ClOH2O and HO2, are 7-10 and 6-9 orders of magnitude slower than the reaction in the absence of water, respectively. cloh2o 72-78 heme oxygenase 2 Homo sapiens 47-50 28960009-6 2018 The most favorable paths, reactions between H2OHO2 and ClO, and between ClOH2O and HO2, are 7-10 and 6-9 orders of magnitude slower than the reaction in the absence of water, respectively. Water 168-173 heme oxygenase 2 Homo sapiens 47-50 29387837-0 2018 H-Abstraction reactions by OH, HO2, O, O2 and benzyl radical addition to O2 and their implications for kinetic modelling of toluene oxidation. Toluene 124-131 heme oxygenase 2 Homo sapiens 31-34 29417107-0 2018 Direct measurement of OH and HO2 formation in R + O2 reactions of cyclohexane and tetrahydropyran. Cyclohexane 69-80 heme oxygenase 2 Homo sapiens 30-33 29417107-0 2018 Direct measurement of OH and HO2 formation in R + O2 reactions of cyclohexane and tetrahydropyran. TETRAHYDROPYRAN 85-100 heme oxygenase 2 Homo sapiens 30-33 29417107-1 2018 Formation of the key general radical chain carriers, OH and HO2 , during pulsed-photolytic Cl-initiated oxidation of tetrahydropyran and cyclohexane are measured with time-resolved infrared absorption in a temperature-controlled Herriott multipass cell in the temperature range of 500-750 K at 20 Torr. radical 29-36 heme oxygenase 2 Homo sapiens 61-64 29417107-1 2018 Formation of the key general radical chain carriers, OH and HO2 , during pulsed-photolytic Cl-initiated oxidation of tetrahydropyran and cyclohexane are measured with time-resolved infrared absorption in a temperature-controlled Herriott multipass cell in the temperature range of 500-750 K at 20 Torr. TETRAHYDROPYRAN 119-134 heme oxygenase 2 Homo sapiens 61-64 29417107-1 2018 Formation of the key general radical chain carriers, OH and HO2 , during pulsed-photolytic Cl-initiated oxidation of tetrahydropyran and cyclohexane are measured with time-resolved infrared absorption in a temperature-controlled Herriott multipass cell in the temperature range of 500-750 K at 20 Torr. Cyclohexane 139-150 heme oxygenase 2 Homo sapiens 61-64 29417107-4 2018 In both cyclohexane and tetrahydropyran oxidation, a faster timescale is strongly related to the "well-skipping" ( R + O2 alkene + HO2 or cyclic ether + OH) mechanism and is expected to have, at most, a weak temperature dependence. Cyclohexane 8-19 heme oxygenase 2 Homo sapiens 133-136 29417107-4 2018 In both cyclohexane and tetrahydropyran oxidation, a faster timescale is strongly related to the "well-skipping" ( R + O2 alkene + HO2 or cyclic ether + OH) mechanism and is expected to have, at most, a weak temperature dependence. TETRAHYDROPYRAN 24-39 heme oxygenase 2 Homo sapiens 133-136 29417107-4 2018 In both cyclohexane and tetrahydropyran oxidation, a faster timescale is strongly related to the "well-skipping" ( R + O2 alkene + HO2 or cyclic ether + OH) mechanism and is expected to have, at most, a weak temperature dependence. r + o2 alkene 115-130 heme oxygenase 2 Homo sapiens 133-136 29417107-4 2018 In both cyclohexane and tetrahydropyran oxidation, a faster timescale is strongly related to the "well-skipping" ( R + O2 alkene + HO2 or cyclic ether + OH) mechanism and is expected to have, at most, a weak temperature dependence. Ethers, Cyclic 141-153 heme oxygenase 2 Homo sapiens 133-136 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Oxygen 18-20 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Oxygen 18-20 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). tetrahydropyranyl 109-126 heme oxygenase 2 Homo sapiens 17-20 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). tetrahydropyranyl 109-126 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). tetrahydropyranyl 109-126 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Oxygen 98-100 heme oxygenase 2 Homo sapiens 17-20 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Oxygen 98-100 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Oxygen 98-100 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Cyclohexane 182-193 heme oxygenase 2 Homo sapiens 17-20 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Cyclohexane 182-193 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Cyclohexane 182-193 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Alkenes 261-267 heme oxygenase 2 Homo sapiens 17-20 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Alkenes 261-267 heme oxygenase 2 Homo sapiens 154-157 29417107-5 2018 Indeed, the fast HO2 formation timescale is nearly temperature independent both for cyclohexyl + O2 and for tetrahydropyranyl + O2 below 700 K. A slower HO2 formation timescale in cyclohexane oxidation is shown to be linked to the sequential R + O2 ROO alkene + HO2 pathway, and displays a strong temperature dependence mainly from the final step (with energy barrier ~32.5 kcal mol-1). Alkenes 261-267 heme oxygenase 2 Homo sapiens 154-157 29417107-6 2018 In contrast, the slower HO2 formation timescale in tetrahydropyran oxidation is surprisingly temperature insensitive across all measured temperatures. TETRAHYDROPYRAN 52-67 heme oxygenase 2 Homo sapiens 24-27 29417107-8 2018 This significant difference of HO2 formation kinetics and OH formation yield for the tetrahydropyran oxidation can arise from contributions related to ring-opening pathways in the tetrahydropyranyl + O2 system that compete with the typical R + O2 reaction scheme. TETRAHYDROPYRAN 87-102 heme oxygenase 2 Homo sapiens 31-34 29417107-8 2018 This significant difference of HO2 formation kinetics and OH formation yield for the tetrahydropyran oxidation can arise from contributions related to ring-opening pathways in the tetrahydropyranyl + O2 system that compete with the typical R + O2 reaction scheme. tetrahydropyranyl + o2 182-204 heme oxygenase 2 Homo sapiens 31-34 29533404-0 2018 Reaction kinetics of hydrogen atom abstraction from isopentanol by the H atom and HO2 radical. Hydrogen 21-29 heme oxygenase 2 Homo sapiens 82-85 29533404-0 2018 Reaction kinetics of hydrogen atom abstraction from isopentanol by the H atom and HO2 radical. isopentyl alcohol 52-63 heme oxygenase 2 Homo sapiens 82-85 29533404-4 2018 In this study, rate constants are determined for the hydrogen atom abstraction reactions from isopentanol by the H atom and HO2 radical by implementing the CBS-QB3 composite method. Hydrogen 53-61 heme oxygenase 2 Homo sapiens 124-127 29533404-4 2018 In this study, rate constants are determined for the hydrogen atom abstraction reactions from isopentanol by the H atom and HO2 radical by implementing the CBS-QB3 composite method. isopentyl alcohol 94-105 heme oxygenase 2 Homo sapiens 124-127 29533404-6 2018 On comparing the computed reaction energies, the highest exothermicity (DeltaE = -46 kJ mol-1) is depicted for Halpha abstraction by the H atom whereas the lowest endothermicity (DeltaE = 29 kJ mol-1) is shown for the abstraction of Halpha by the HO2 radical. halpha 111-117 heme oxygenase 2 Homo sapiens 247-250 29533404-7 2018 The formation of hydrogen bonding is found to affect the kinetics of the H atom abstraction reactions by the HO2 radical. Hydrogen 17-25 heme oxygenase 2 Homo sapiens 109-112 29533404-8 2018 Further above 750 K, the calculated high pressure limit rate constants indicate that the total contribution from delta carbon sites (Cdelta) is predominant for hydrogen atom abstraction by the H atom and HO2 radical. Carbon 119-125 heme oxygenase 2 Homo sapiens 204-207 29533404-8 2018 Further above 750 K, the calculated high pressure limit rate constants indicate that the total contribution from delta carbon sites (Cdelta) is predominant for hydrogen atom abstraction by the H atom and HO2 radical. Hydrogen 160-168 heme oxygenase 2 Homo sapiens 204-207 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Reactive Oxygen Species 24-27 heme oxygenase 2 Homo sapiens 151-155 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Hydrogen Sulfide 31-34 heme oxygenase 2 Homo sapiens 133-149 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Hydrogen Sulfide 31-34 heme oxygenase 2 Homo sapiens 151-155 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Carbon Monoxide 160-175 heme oxygenase 2 Homo sapiens 133-149 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Carbon Monoxide 160-175 heme oxygenase 2 Homo sapiens 151-155 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Carbon Monoxide 177-179 heme oxygenase 2 Homo sapiens 133-149 29470646-8 2018 However, the effects of ROS on H2S production are not due to direct effects on CSE enzyme activity but rather due to inactivation of heme oxygenase-2 (HO-2), a carbon monoxide (CO) producing enzyme. Carbon Monoxide 177-179 heme oxygenase 2 Homo sapiens 151-155 29470646-10 2018 During IH, reduced CO production resulting from inactivation of HO-2 by ROS releases the inhibition of CO on CSE thereby increasing H2S. Reactive Oxygen Species 72-75 heme oxygenase 2 Homo sapiens 64-68 29470646-10 2018 During IH, reduced CO production resulting from inactivation of HO-2 by ROS releases the inhibition of CO on CSE thereby increasing H2S. Hydrogen Sulfide 132-135 heme oxygenase 2 Homo sapiens 64-68 28942315-8 2018 The chemically produced HO2 was largely converted to OH by the reactions with NO (HO2+NO=OH+NO2) from BB emissions. boeravinone B 102-104 heme oxygenase 2 Homo sapiens 24-27 29390173-4 2018 The rates for accretion product formation are very high for RO2 radicals bearing functional groups, competing with those of the corresponding reactions with NO and HO2 . ro2 radicals 60-72 heme oxygenase 2 Homo sapiens 164-167 29520400-0 2018 Role of the (H2O)n (n = 1-3) cluster in the HO2 + HO 3O2 + H2O reaction: mechanistic and kinetic studies. Water 13-16 heme oxygenase 2 Homo sapiens 44-47 29520400-0 2018 Role of the (H2O)n (n = 1-3) cluster in the HO2 + HO 3O2 + H2O reaction: mechanistic and kinetic studies. Water 60-63 heme oxygenase 2 Homo sapiens 44-47 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. (h2o)n 44-50 heme oxygenase 2 Homo sapiens 137-140 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. (h2o)n 44-50 heme oxygenase 2 Homo sapiens 161-164 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. Water 45-48 heme oxygenase 2 Homo sapiens 137-140 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. Water 45-48 heme oxygenase 2 Homo sapiens 161-164 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. CHEMBL1771216 87-90 heme oxygenase 2 Homo sapiens 137-140 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. CHEMBL1771216 87-90 heme oxygenase 2 Homo sapiens 161-164 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. Holmium 132-134 heme oxygenase 2 Homo sapiens 137-140 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. Holmium 132-134 heme oxygenase 2 Homo sapiens 161-164 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. ho(h2o) 167-174 heme oxygenase 2 Homo sapiens 137-140 29520400-2 2018 Our results show that upon incorporation of (H2O)n (n = 1-3) into the channel of H2O + 3O2 formation, two different reactions, i.e. HO + HO2(H2O)n (n = 1-3) and HO2 + HO(H2O)n (n = 1-3), have been observed, and these two reactions are competitive with each other. ho(h2o) 167-174 heme oxygenase 2 Homo sapiens 161-164 28942315-4 2018 In the early period of transport, high NOx and VOCs emissions caused O3 production due to reactions with the peroxide and hydroxyl radicals, HO2 and OH. nicotine 1-N-oxide 39-42 heme oxygenase 2 Homo sapiens 141-144 28942315-4 2018 In the early period of transport, high NOx and VOCs emissions caused O3 production due to reactions with the peroxide and hydroxyl radicals, HO2 and OH. Ozone 69-71 heme oxygenase 2 Homo sapiens 141-144 28942315-6 2018 The results indicated that HO2 in the BB plume primarily came from formaldehyde (HCHO+hv=2HO2+CO), a secondary alkoxy radical (ROR=HO2). Formaldehyde 67-79 heme oxygenase 2 Homo sapiens 27-30 28942315-6 2018 The results indicated that HO2 in the BB plume primarily came from formaldehyde (HCHO+hv=2HO2+CO), a secondary alkoxy radical (ROR=HO2). Carbon Monoxide 94-96 heme oxygenase 2 Homo sapiens 27-30 28942315-6 2018 The results indicated that HO2 in the BB plume primarily came from formaldehyde (HCHO+hv=2HO2+CO), a secondary alkoxy radical (ROR=HO2). alkoxy radical 111-125 heme oxygenase 2 Homo sapiens 27-30 28942315-7 2018 CO played an important role in the production of recycled HO2 (OH+CO=HO2) because of its abundance in the BB plume. 3-hydroxy-5-cholen-24-oic acid 3-sulfate ester 63-68 heme oxygenase 2 Homo sapiens 58-61 28942315-8 2018 The chemically produced HO2 was largely converted to OH by the reactions with NO (HO2+NO=OH+NO2) from BB emissions. boeravinone B 102-104 heme oxygenase 2 Homo sapiens 82-85 28942315-7 2018 CO played an important role in the production of recycled HO2 (OH+CO=HO2) because of its abundance in the BB plume. 3-hydroxy-5-cholen-24-oic acid 3-sulfate ester 63-68 heme oxygenase 2 Homo sapiens 69-72 28942315-9 2018 This is in contrast to the surface, where HO2 and OH are strongly affected by VOC and HONO, respectively. Nitrous Acid 86-90 heme oxygenase 2 Homo sapiens 42-45 28942315-8 2018 The chemically produced HO2 was largely converted to OH by the reactions with NO (HO2+NO=OH+NO2) from BB emissions. Nitrogen Dioxide 92-95 heme oxygenase 2 Homo sapiens 24-27 29206257-2 2017 In this work, the interactions of H2O and/or O2 with BP are investigated using first-principles calculations. Phosphorus 53-55 heme oxygenase 2 Homo sapiens 34-47 28942315-8 2018 The chemically produced HO2 was largely converted to OH by the reactions with NO (HO2+NO=OH+NO2) from BB emissions. Nitrogen Dioxide 92-95 heme oxygenase 2 Homo sapiens 82-85 29206257-6 2017 The effects of H2O and/or O2 on the quasiparticle band gap and exciton binding energy of BP are also investigated. Phosphorus 89-91 heme oxygenase 2 Homo sapiens 15-28 29164345-0 2017 Ab initio molecular dynamics of the reactivity of vitamin C toward hydroxyl and HO2/O-2 radicals. Ascorbic Acid 50-59 heme oxygenase 2 Homo sapiens 80-87 28493625-1 2017 We report measurements of hydroxyl (OH) and hydroperoxy (HO2 ) radicals made by laser-induced fluorescence spectroscopy in a computer classroom (i) in the absence of indoor activities (ii) during desk cleaning with a limonene-containing cleaner (iii) during operation of a commercially available "air cleaning" device. hydroperoxy 44-55 heme oxygenase 2 Homo sapiens 57-60 28493625-1 2017 We report measurements of hydroxyl (OH) and hydroperoxy (HO2 ) radicals made by laser-induced fluorescence spectroscopy in a computer classroom (i) in the absence of indoor activities (ii) during desk cleaning with a limonene-containing cleaner (iii) during operation of a commercially available "air cleaning" device. Limonene 217-225 heme oxygenase 2 Homo sapiens 57-60 28796517-0 2017 Computational and Experimental Investigation of the Detection of HO2 Radical and the Products of Its Reaction with Cyclohexene Ozonolysis Derived RO2 Radicals by an Iodide-Based Chemical Ionization Mass Spectrometer. cyclohexene 115-126 heme oxygenase 2 Homo sapiens 65-68 28796517-0 2017 Computational and Experimental Investigation of the Detection of HO2 Radical and the Products of Its Reaction with Cyclohexene Ozonolysis Derived RO2 Radicals by an Iodide-Based Chemical Ionization Mass Spectrometer. ro2 radicals 146-158 heme oxygenase 2 Homo sapiens 65-68 28796517-0 2017 Computational and Experimental Investigation of the Detection of HO2 Radical and the Products of Its Reaction with Cyclohexene Ozonolysis Derived RO2 Radicals by an Iodide-Based Chemical Ionization Mass Spectrometer. Iodides 165-171 heme oxygenase 2 Homo sapiens 65-68 28796517-2 2017 In this work, we demonstrate the direct detection of the HO2 radical using an iodide-based chemical ionization mass spectrometer (iodide-CIMS). Iodides 78-84 heme oxygenase 2 Homo sapiens 57-60 28796517-2 2017 In this work, we demonstrate the direct detection of the HO2 radical using an iodide-based chemical ionization mass spectrometer (iodide-CIMS). iodide-cims 130-141 heme oxygenase 2 Homo sapiens 57-60 28796517-5 2017 The ozone-initiated cyclohexene oxidation mechanism was perturbed by the introduction of the HO2 radical, leading to the formation of closed-shell hydroperoxides. cyclohexene 20-31 heme oxygenase 2 Homo sapiens 93-96 28796517-5 2017 The ozone-initiated cyclohexene oxidation mechanism was perturbed by the introduction of the HO2 radical, leading to the formation of closed-shell hydroperoxides. Hydrogen Peroxide 147-161 heme oxygenase 2 Homo sapiens 93-96 28544901-2 2017 The highly graphitized multi-walled carbon nanotubes g-MWCNTs modified electrode was prepared for the in-situ electrochemical generation of HO2-. Carbon 36-42 heme oxygenase 2 Homo sapiens 140-143 28544901-5 2017 Large amount of reactive oxygen species (HO2- and OH) were in-situ electro-generated from the two-electron oxygen reduction and chromium-induced alkaline electro-Fenton-like reaction. Reactive Oxygen Species 16-39 heme oxygenase 2 Homo sapiens 41-44 28544901-5 2017 Large amount of reactive oxygen species (HO2- and OH) were in-situ electro-generated from the two-electron oxygen reduction and chromium-induced alkaline electro-Fenton-like reaction. Oxygen 25-31 heme oxygenase 2 Homo sapiens 41-44 28544901-5 2017 Large amount of reactive oxygen species (HO2- and OH) were in-situ electro-generated from the two-electron oxygen reduction and chromium-induced alkaline electro-Fenton-like reaction. Chromium 129-137 heme oxygenase 2 Homo sapiens 41-44 28527438-5 2017 At 0 K, the minimum energy R + O2 pathway involves direct elimination of HO2 (30.3 kcal mol-1 barrier) from the tert-butyl peroxy radical (ROO ) to give isobutene. Oxygen 32-34 heme oxygenase 2 Homo sapiens 74-77 28825741-0 2017 Kinetics of the BrO + HO2 reaction over the temperature range T = 246-314 K. The kinetics of the reaction between gas phase BrO and HO2 radicals, BrO + HO2 HOBr + O2 (1), have been studied over the atmospherically relevant temperature range T = 246-314 K and at ambient pressure, p = 760 +- 20 Torr, using laser flash photolysis coupled with ultraviolet absorption spectroscopy. bromosyl 16-19 heme oxygenase 2 Homo sapiens 22-25 28825741-0 2017 Kinetics of the BrO + HO2 reaction over the temperature range T = 246-314 K. The kinetics of the reaction between gas phase BrO and HO2 radicals, BrO + HO2 HOBr + O2 (1), have been studied over the atmospherically relevant temperature range T = 246-314 K and at ambient pressure, p = 760 +- 20 Torr, using laser flash photolysis coupled with ultraviolet absorption spectroscopy. bromosyl 16-19 heme oxygenase 2 Homo sapiens 132-135 28825741-0 2017 Kinetics of the BrO + HO2 reaction over the temperature range T = 246-314 K. The kinetics of the reaction between gas phase BrO and HO2 radicals, BrO + HO2 HOBr + O2 (1), have been studied over the atmospherically relevant temperature range T = 246-314 K and at ambient pressure, p = 760 +- 20 Torr, using laser flash photolysis coupled with ultraviolet absorption spectroscopy. bromosyl 16-19 heme oxygenase 2 Homo sapiens 132-135 28825741-0 2017 Kinetics of the BrO + HO2 reaction over the temperature range T = 246-314 K. The kinetics of the reaction between gas phase BrO and HO2 radicals, BrO + HO2 HOBr + O2 (1), have been studied over the atmospherically relevant temperature range T = 246-314 K and at ambient pressure, p = 760 +- 20 Torr, using laser flash photolysis coupled with ultraviolet absorption spectroscopy. hypobromous acid 158-162 heme oxygenase 2 Homo sapiens 22-25 28825741-0 2017 Kinetics of the BrO + HO2 reaction over the temperature range T = 246-314 K. The kinetics of the reaction between gas phase BrO and HO2 radicals, BrO + HO2 HOBr + O2 (1), have been studied over the atmospherically relevant temperature range T = 246-314 K and at ambient pressure, p = 760 +- 20 Torr, using laser flash photolysis coupled with ultraviolet absorption spectroscopy. Oxygen 23-25 heme oxygenase 2 Homo sapiens 132-135 28825741-0 2017 Kinetics of the BrO + HO2 reaction over the temperature range T = 246-314 K. The kinetics of the reaction between gas phase BrO and HO2 radicals, BrO + HO2 HOBr + O2 (1), have been studied over the atmospherically relevant temperature range T = 246-314 K and at ambient pressure, p = 760 +- 20 Torr, using laser flash photolysis coupled with ultraviolet absorption spectroscopy. Oxygen 23-25 heme oxygenase 2 Homo sapiens 132-135 28825741-2 2017 Subsequently, the addition of methanol vapour to the reaction mixture, in the presence of excess oxygen, afforded the efficient simultaneous post-photolysis formation of HO2 radicals using well-defined chemistry. Methanol 30-38 heme oxygenase 2 Homo sapiens 170-173 28825741-2 2017 Subsequently, the addition of methanol vapour to the reaction mixture, in the presence of excess oxygen, afforded the efficient simultaneous post-photolysis formation of HO2 radicals using well-defined chemistry. Oxygen 97-103 heme oxygenase 2 Homo sapiens 170-173 28825741-3 2017 The decay of BrO radicals, in the presence and absence of HO2, was interrogated to determine the rate coefficients for the BrO + BrO and the BrO + HO2 reactions. bromosyl 13-16 heme oxygenase 2 Homo sapiens 147-150 28771354-1 2017 We report a systematic chemical kinetics study of the H atom abstractions from ethyl formate (EF) by H, O(3P), CH3, OH, and HO2 radicals. ethyl formate 79-92 heme oxygenase 2 Homo sapiens 124-127 28458003-7 2017 Results indicated that benzene and sabinene reacted with ozone to produce a range of stable products and intermediates, including carbocations, ring-scission products, as well as peroxy (HO2 and HO3) and hydroxyl (OH) radicals. Benzene 23-30 heme oxygenase 2 Homo sapiens 187-190 28458003-7 2017 Results indicated that benzene and sabinene reacted with ozone to produce a range of stable products and intermediates, including carbocations, ring-scission products, as well as peroxy (HO2 and HO3) and hydroxyl (OH) radicals. sabinene 35-43 heme oxygenase 2 Homo sapiens 187-190 28527438-5 2017 At 0 K, the minimum energy R + O2 pathway involves direct elimination of HO2 (30.3 kcal mol-1 barrier) from the tert-butyl peroxy radical (ROO ) to give isobutene. tert-butyl peroxy radical 114-139 heme oxygenase 2 Homo sapiens 74-77 28527438-5 2017 At 0 K, the minimum energy R + O2 pathway involves direct elimination of HO2 (30.3 kcal mol-1 barrier) from the tert-butyl peroxy radical (ROO ) to give isobutene. roo 141-144 heme oxygenase 2 Homo sapiens 74-77 28527438-5 2017 At 0 K, the minimum energy R + O2 pathway involves direct elimination of HO2 (30.3 kcal mol-1 barrier) from the tert-butyl peroxy radical (ROO ) to give isobutene. isobutylene 155-164 heme oxygenase 2 Homo sapiens 74-77 28202267-3 2017 Comparison of the LES results from two chemical schemes (simple NOx-O3 chemistry and a more comprehensive Reduced Chemical Scheme (RCS) chemical mechanism) shows that the concentrations of NO2 and Ox inside the street canyon are enhanced by approximately 30-40% via OH/HO2 chemistry. Nitrogen Dioxide 189-192 heme oxygenase 2 Homo sapiens 269-272 28388039-4 2017 Furthermore, these calculations suggest that the dominant product of this isomerization is a dihydroxy hydroperoxy epoxide (C5H10O5), which is expected to have a saturation vapor pressure ~2 orders of magnitude higher, as determined by group-contribution calculations, than the dihydroxy dihydroperoxide, ISOP(OOH)2(C5H12O6), a major product of the peroxy radical reacting with HO2. dihydroxy hydroperoxy epoxide 93-122 heme oxygenase 2 Homo sapiens 378-381 28388039-4 2017 Furthermore, these calculations suggest that the dominant product of this isomerization is a dihydroxy hydroperoxy epoxide (C5H10O5), which is expected to have a saturation vapor pressure ~2 orders of magnitude higher, as determined by group-contribution calculations, than the dihydroxy dihydroperoxide, ISOP(OOH)2(C5H12O6), a major product of the peroxy radical reacting with HO2. L-xylose 124-131 heme oxygenase 2 Homo sapiens 378-381 28394125-6 2017 Alternatively, these radicals would react directly with O3, NO2, HO2/RO2, etc. ro2 69-72 heme oxygenase 2 Homo sapiens 65-68 28121426-3 2017 The HO2 yield has been obtained from simultaneous time-resolved measurements of the absolute concentration of CH3O2, OH, and HO2 radicals by cw-CRDS. Methyldioxy radical 110-115 heme oxygenase 2 Homo sapiens 4-7 28276576-2 2017 Our group reported decreased risk for ET in carriers of the minor alleles of the rs2071746 and rs1051308 SNPs in the haem-oxygenases 1 and 2 (HMOX1 and HMOX2), respectively, involved in haem metabolism. Heme 117-121 heme oxygenase 2 Homo sapiens 152-157 28252954-7 2017 The approach is illustrated for the redox couples Fe2+/Fe3+, HO2 /HO2-, and MnO4-/MnO4-2 in aqueous solution and yields redox potentials differing by less than 0.1 eV from respective ones achieved with the thermodynamic integration method. ammonium ferrous sulfate 50-54 heme oxygenase 2 Homo sapiens 61-64 28252954-7 2017 The approach is illustrated for the redox couples Fe2+/Fe3+, HO2 /HO2-, and MnO4-/MnO4-2 in aqueous solution and yields redox potentials differing by less than 0.1 eV from respective ones achieved with the thermodynamic integration method. ammonium ferrous sulfate 50-54 heme oxygenase 2 Homo sapiens 66-69 28480030-1 2017 Carbon monoxide (CO) formed endogenously is considered to be cytoprotective, and the vast majority of CO formation is attributed to the degradation of heme by heme oxygenases-1 and -2 (HO-1, HO-2). Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 191-195 28480030-1 2017 Carbon monoxide (CO) formed endogenously is considered to be cytoprotective, and the vast majority of CO formation is attributed to the degradation of heme by heme oxygenases-1 and -2 (HO-1, HO-2). Heme 151-155 heme oxygenase 2 Homo sapiens 191-195 28480030-2 2017 Previously, we observed that brain microsomes containing HO-2 produced many-fold more CO in the presence of menadione and its congeners; herein we explored these observations further. Vitamin K 3 108-117 heme oxygenase 2 Homo sapiens 57-61 28207262-0 2017 First-Principles Chemical Kinetic Modeling of Methyl trans-3-Hexenoate Epoxidation by HO2. Methyl (E)-hex-3-enoate 46-70 heme oxygenase 2 Homo sapiens 86-89 28207262-3 2017 The obtained rate constants are in good agreement with experimental data for alkene epoxidation by HO2. Alkenes 77-83 heme oxygenase 2 Homo sapiens 99-102 28366987-4 2017 H2O2 was generated simultaneously in this reaction mixture probably from the hydroperoxy radical (HO2 ), which is equilibrated with O2 - in an aqueous condition, and then H2O2 consumed O2 -. Hydrogen Peroxide 0-4 heme oxygenase 2 Homo sapiens 98-101 28366987-4 2017 H2O2 was generated simultaneously in this reaction mixture probably from the hydroperoxy radical (HO2 ), which is equilibrated with O2 - in an aqueous condition, and then H2O2 consumed O2 -. perhydroxyl radical 77-96 heme oxygenase 2 Homo sapiens 98-101 28366987-4 2017 H2O2 was generated simultaneously in this reaction mixture probably from the hydroperoxy radical (HO2 ), which is equilibrated with O2 - in an aqueous condition, and then H2O2 consumed O2 -. Superoxides 2-4 heme oxygenase 2 Homo sapiens 98-101 28411610-0 2017 Benchmark study of the structural and spectroscopic parameters of the hydroxymethyl peroxy (HOCH2OO) radical and its decomposition reaction to HO2 and H2CO. hydroxymethyl peroxy (hoch2oo) radical 70-108 heme oxygenase 2 Homo sapiens 143-146 28121426-7 2017 Inclusion of the CH3O2+OH reaction into the model results in up to 30% decrease in the CH3O2 radical concentration while the HO2 concentration increased by up to 20%. Methyldioxy radical 17-22 heme oxygenase 2 Homo sapiens 125-128 28132836-5 2017 A crystal structure revealed that HO-2 binds myristate via a hydrophobic channel adjacent to the heme-binding pocket. Heme 97-101 heme oxygenase 2 Homo sapiens 34-38 27785502-0 2016 A theoretical study of the atmospherically important radical-radical reaction BrO + HO2; the product channel O2(a1Deltag) + HOBr is formed with the highest rate. hypobromous acid 124-128 heme oxygenase 2 Homo sapiens 84-87 28496972-3 2017 The HO and HO2 originating from both Fenton"s reagent and VUV photolysis of water were identified with suitable radical scavengers. Water 78-83 heme oxygenase 2 Homo sapiens 12-15 28005355-4 2017 The rate coefficients calculated over the 6 x 10-4 - 400 bar range are smaller at least in a factor of about 60 than the consensus value determined for the main reaction channel HO + HO2 H2O + O2, indicating that the recombination pathway is irrelevant. Water 189-192 heme oxygenase 2 Homo sapiens 183-186 27892575-6 2016 The transition from the FeN4 structure to metallic Fe results in a significant loss in ORR activity and an increase in the production of undesirable HO2- during catalysis. fen4 24-28 heme oxygenase 2 Homo sapiens 149-152 27892575-6 2016 The transition from the FeN4 structure to metallic Fe results in a significant loss in ORR activity and an increase in the production of undesirable HO2- during catalysis. Iron 24-26 heme oxygenase 2 Homo sapiens 149-152 28098324-1 2017 Polar solvents like water support the bulk dissociation of themselves and their solutes into ions, and the re-association of these ions into neutral molecules in a dynamic equilibrium, e.g., H2O2 H+ + HO2-. Water 20-25 heme oxygenase 2 Homo sapiens 203-206 28098324-1 2017 Polar solvents like water support the bulk dissociation of themselves and their solutes into ions, and the re-association of these ions into neutral molecules in a dynamic equilibrium, e.g., H2O2 H+ + HO2-. Hydrogen Peroxide 191-195 heme oxygenase 2 Homo sapiens 203-206 28288300-17 2017 were detected from acidic and neutral bleaching agent (30% acidic and neutral H2O2, 35%CP); both HO2. Hydrogen Peroxide 78-82 heme oxygenase 2 Homo sapiens 97-100 28288300-23 2017 RIV for HO2.was maximum at 0min irradiation of alkaline 30%H2O2 and minimum at 2min irradiation of SPT. Hydrogen Peroxide 59-63 heme oxygenase 2 Homo sapiens 8-11 27785502-1 2016 A theoretical study has been made of the BrO + HO2 reaction, a radical-radical reaction which contributes to ozone depletion in the atmosphere via production of HOBr. hypobromous acid 161-165 heme oxygenase 2 Homo sapiens 47-50 27709901-6 2016 The photochemical formation of H2O2 followed the conservative mixing model due to the reaction of C60 - with HO2 /O2 -, and the biomolecular reaction rate constant has been measured as (7.4 +- 0.6) x 106 M-1 s-1. Hydrogen Peroxide 31-35 heme oxygenase 2 Homo sapiens 109-112 27723341-0 2016 Reaction Kinetics of HBr with HO2: A New Channel for Isotope Scrambling Reactions. Hydrobromic Acid 21-24 heme oxygenase 2 Homo sapiens 30-33 27723341-1 2016 The gas phase reaction kinetics of HBr with the HO2 radical are investigated over the temperature range of T = 200-1500 K using a theoretical approach based on transition state theory. Hydrobromic Acid 35-38 heme oxygenase 2 Homo sapiens 48-51 27723341-3 2016 The rate coefficient for the HBr + HO2 Br + H2O2 abstraction channel is found to be somewhat larger than previous estimates at low temperatures due to quantum tunneling. Hydrogen Peroxide 46-50 heme oxygenase 2 Homo sapiens 35-38 27709901-6 2016 The photochemical formation of H2O2 followed the conservative mixing model due to the reaction of C60 - with HO2 /O2 -, and the biomolecular reaction rate constant has been measured as (7.4 +- 0.6) x 106 M-1 s-1. Oxygen 33-35 heme oxygenase 2 Homo sapiens 109-112 27510308-1 2016 The PERCA (PEroxy Radical Chemical Amplification) technique, which is based on the catalytic conversion of ambient peroxy radicals (HO2 and RO2, where R stands for any organic chain) to a larger amount of nitrogen dioxide (NO2) amplified by chain reactions by adding high concentrations of NO and CO in the flow reactor, has been widely used for total peroxy radical RO2* (RO2* = HO2 + SigmaRO2) measurements. peroxy radicals 115-130 heme oxygenase 2 Homo sapiens 132-135 27510308-1 2016 The PERCA (PEroxy Radical Chemical Amplification) technique, which is based on the catalytic conversion of ambient peroxy radicals (HO2 and RO2, where R stands for any organic chain) to a larger amount of nitrogen dioxide (NO2) amplified by chain reactions by adding high concentrations of NO and CO in the flow reactor, has been widely used for total peroxy radical RO2* (RO2* = HO2 + SigmaRO2) measurements. peroxy radicals 115-130 heme oxygenase 2 Homo sapiens 380-383 27510308-1 2016 The PERCA (PEroxy Radical Chemical Amplification) technique, which is based on the catalytic conversion of ambient peroxy radicals (HO2 and RO2, where R stands for any organic chain) to a larger amount of nitrogen dioxide (NO2) amplified by chain reactions by adding high concentrations of NO and CO in the flow reactor, has been widely used for total peroxy radical RO2* (RO2* = HO2 + SigmaRO2) measurements. Nitrogen Dioxide 205-221 heme oxygenase 2 Homo sapiens 380-383 27510308-1 2016 The PERCA (PEroxy Radical Chemical Amplification) technique, which is based on the catalytic conversion of ambient peroxy radicals (HO2 and RO2, where R stands for any organic chain) to a larger amount of nitrogen dioxide (NO2) amplified by chain reactions by adding high concentrations of NO and CO in the flow reactor, has been widely used for total peroxy radical RO2* (RO2* = HO2 + SigmaRO2) measurements. Nitrogen Dioxide 205-221 heme oxygenase 2 Homo sapiens 132-135 27510308-1 2016 The PERCA (PEroxy Radical Chemical Amplification) technique, which is based on the catalytic conversion of ambient peroxy radicals (HO2 and RO2, where R stands for any organic chain) to a larger amount of nitrogen dioxide (NO2) amplified by chain reactions by adding high concentrations of NO and CO in the flow reactor, has been widely used for total peroxy radical RO2* (RO2* = HO2 + SigmaRO2) measurements. Nitrogen Dioxide 223-226 heme oxygenase 2 Homo sapiens 380-383 27510308-1 2016 The PERCA (PEroxy Radical Chemical Amplification) technique, which is based on the catalytic conversion of ambient peroxy radicals (HO2 and RO2, where R stands for any organic chain) to a larger amount of nitrogen dioxide (NO2) amplified by chain reactions by adding high concentrations of NO and CO in the flow reactor, has been widely used for total peroxy radical RO2* (RO2* = HO2 + SigmaRO2) measurements. Oxygen 115-129 heme oxygenase 2 Homo sapiens 132-135 27510308-1 2016 The PERCA (PEroxy Radical Chemical Amplification) technique, which is based on the catalytic conversion of ambient peroxy radicals (HO2 and RO2, where R stands for any organic chain) to a larger amount of nitrogen dioxide (NO2) amplified by chain reactions by adding high concentrations of NO and CO in the flow reactor, has been widely used for total peroxy radical RO2* (RO2* = HO2 + SigmaRO2) measurements. Oxygen 115-129 heme oxygenase 2 Homo sapiens 380-383 27711723-1 2016 Structures and binding energies of the sequential addition of CO, H2O, O2, and N2 onto Au. Gold 87-89 heme oxygenase 2 Homo sapiens 66-81 27711756-0 2016 A series of dinuclear lanthanide complexes with slow magnetic relaxation for Dy2 and Ho2. dinuclear lanthanide 12-32 heme oxygenase 2 Homo sapiens 85-88 27173532-2 2016 Superoxide radicals (O2(*-)) and their protonated form (hydroperoxyl radicals, HO2(*)) were detected by the reduction of nitroblue tetrazolium into formazan, and hydroxyl radicals (OH(*)) were detected by the hydroxylation of terephthalate. Superoxides 0-19 heme oxygenase 2 Homo sapiens 79-82 27173532-2 2016 Superoxide radicals (O2(*-)) and their protonated form (hydroperoxyl radicals, HO2(*)) were detected by the reduction of nitroblue tetrazolium into formazan, and hydroxyl radicals (OH(*)) were detected by the hydroxylation of terephthalate. Nitroblue Tetrazolium 121-142 heme oxygenase 2 Homo sapiens 79-82 27173532-2 2016 Superoxide radicals (O2(*-)) and their protonated form (hydroperoxyl radicals, HO2(*)) were detected by the reduction of nitroblue tetrazolium into formazan, and hydroxyl radicals (OH(*)) were detected by the hydroxylation of terephthalate. Formazans 148-156 heme oxygenase 2 Homo sapiens 79-82 27173532-2 2016 Superoxide radicals (O2(*-)) and their protonated form (hydroperoxyl radicals, HO2(*)) were detected by the reduction of nitroblue tetrazolium into formazan, and hydroxyl radicals (OH(*)) were detected by the hydroxylation of terephthalate. Hydroxyl Radical 162-179 heme oxygenase 2 Homo sapiens 79-82 27173532-2 2016 Superoxide radicals (O2(*-)) and their protonated form (hydroperoxyl radicals, HO2(*)) were detected by the reduction of nitroblue tetrazolium into formazan, and hydroxyl radicals (OH(*)) were detected by the hydroxylation of terephthalate. terephthalic acid 226-239 heme oxygenase 2 Homo sapiens 79-82 27173532-3 2016 Under gastric conditions, O2(*-)/HO2(*) were detected in higher quantity than OH(*). Superoxides 26-28 heme oxygenase 2 Homo sapiens 33-36 27552660-0 2016 Potential Energy Surfaces for the Reactions of HO2 Radical with CH2O and HO2 in CO2 Environment. Formaldehyde 64-68 heme oxygenase 2 Homo sapiens 47-50 27552660-0 2016 Potential Energy Surfaces for the Reactions of HO2 Radical with CH2O and HO2 in CO2 Environment. Carbon Dioxide 80-83 heme oxygenase 2 Homo sapiens 47-50 27552660-0 2016 Potential Energy Surfaces for the Reactions of HO2 Radical with CH2O and HO2 in CO2 Environment. Carbon Dioxide 80-83 heme oxygenase 2 Homo sapiens 73-76 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. Hydrogen 122-130 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. Hydroperoxy radical 153-173 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. Formaldehyde 179-191 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. Formaldehyde 192-196 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. 7 alpha-hydroxy-4-cholesten-3-one 205-208 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. Hydrogen Peroxide 211-215 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. hydroperoxyl radical 2ho2 228-253 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. Hydrogen Peroxide 256-260 heme oxygenase 2 Homo sapiens 199-202 27552660-1 2016 We report on potential energies for the transition state, reactant, and product complexes along the reaction pathways for hydrogen transfer reactions to hydroperoxyl radical from formaldehyde H2CO + HO2 HCO + H2O2 and another hydroperoxyl radical 2HO2 H2O2 + O2 in the presence of one carbon dioxide molecule. Carbon Dioxide 289-303 heme oxygenase 2 Homo sapiens 199-202 27552660-5 2016 This indicates that CO2 environment is likely to have catalytic effect on HO2 self-reaction, which needs to be included in kinetic combustion mechanisms in supercritical CO2. Carbon Dioxide 20-23 heme oxygenase 2 Homo sapiens 74-77 27552660-5 2016 This indicates that CO2 environment is likely to have catalytic effect on HO2 self-reaction, which needs to be included in kinetic combustion mechanisms in supercritical CO2. Carbon Dioxide 170-173 heme oxygenase 2 Homo sapiens 74-77 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Heme 96-100 heme oxygenase 2 Homo sapiens 56-61 27588691-5 2016 Furthermore, spin trapping technique directly detected the oxidizing species such as OH, HO2 , and 1O2 in the visible light irradiated solution of RhB/fullerol mixture. rhb 148-151 heme oxygenase 2 Homo sapiens 90-93 27588691-5 2016 Furthermore, spin trapping technique directly detected the oxidizing species such as OH, HO2 , and 1O2 in the visible light irradiated solution of RhB/fullerol mixture. fullerol 152-160 heme oxygenase 2 Homo sapiens 90-93 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Carbon Monoxide 104-119 heme oxygenase 2 Homo sapiens 56-61 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Carbon Monoxide 121-123 heme oxygenase 2 Homo sapiens 56-61 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Iron 126-138 heme oxygenase 2 Homo sapiens 56-61 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Biliverdine 144-154 heme oxygenase 2 Homo sapiens 56-61 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Bilirubin 205-214 heme oxygenase 2 Homo sapiens 56-61 27465104-2 2016 Hydroperoxyl radical (HO2 (.) Hydroperoxy radical 0-20 heme oxygenase 2 Homo sapiens 22-25 27556141-7 2016 An absorption cross section of sigmaOH = (1.54 +- 0.1) x 10(-19) cm(2) at a total pressure of 50 Torr helium has been obtained from consistent fitting of OH and HO2 profiles in a large range of concentrations. sigmaoh 31-38 heme oxygenase 2 Homo sapiens 161-164 29619286-8 2016 We also find that MCM v3.3.1 may underestimate glyoxal production from isoprene oxidation, in part due to an underestimated yield from the reaction of IEPOX peroxy radicals (IEPOXOO) with HO2. Glyoxal 47-54 heme oxygenase 2 Homo sapiens 188-191 27580251-9 2016 From the simulation results, ethanol + HO2 was identified as an important reaction at the experimental conditions for both the ignition delay time and intermediate species measurements. Ethanol 29-36 heme oxygenase 2 Homo sapiens 39-42 27580251-10 2016 Further studies to improve the accuracy of the rate coefficient for ethanol + HO2 would improve the predictive understanding of intermediate and low-temperature ethanol combustion. Ethanol 161-168 heme oxygenase 2 Homo sapiens 78-81 27529639-0 2016 Predicted Chemical Activation Rate Constants for HO2 + CH2NH: The Dominant Role of a Hydrogen-Bonded Pre-reactive Complex. Hydrogen 85-93 heme oxygenase 2 Homo sapiens 49-52 27529639-1 2016 The reaction of methanimine (CH2NH) with the hydroperoxy (HO2) radical has been investigated by using a combination of ab initio and density functional theory (CCSD(T)/CBSB7//B3LYP+Dispersion/CBSB7) and master equation calculations based on transition state theory (TST). methyleneimine 16-27 heme oxygenase 2 Homo sapiens 58-61 27529639-1 2016 The reaction of methanimine (CH2NH) with the hydroperoxy (HO2) radical has been investigated by using a combination of ab initio and density functional theory (CCSD(T)/CBSB7//B3LYP+Dispersion/CBSB7) and master equation calculations based on transition state theory (TST). ch2nh 29-34 heme oxygenase 2 Homo sapiens 58-61 27529639-9 2016 The kinetics of the HO2 + CH2NH reaction system differs substantially from the analogous isoelectronic reaction systems involving C2H4 and CH2O, which have been the subjects of previous experimental and theoretical studies. ch2nh 26-31 heme oxygenase 2 Homo sapiens 20-23 27529639-9 2016 The kinetics of the HO2 + CH2NH reaction system differs substantially from the analogous isoelectronic reaction systems involving C2H4 and CH2O, which have been the subjects of previous experimental and theoretical studies. ethylene 130-134 heme oxygenase 2 Homo sapiens 20-23 27529639-9 2016 The kinetics of the HO2 + CH2NH reaction system differs substantially from the analogous isoelectronic reaction systems involving C2H4 and CH2O, which have been the subjects of previous experimental and theoretical studies. Formaldehyde 139-143 heme oxygenase 2 Homo sapiens 20-23 29619286-8 2016 We also find that MCM v3.3.1 may underestimate glyoxal production from isoprene oxidation, in part due to an underestimated yield from the reaction of IEPOX peroxy radicals (IEPOXOO) with HO2. iepox peroxy radicals 151-172 heme oxygenase 2 Homo sapiens 188-191 27465104-7 2016 abstracts hydrogen rapidly from H2 O2 to produce HO2 (.) Hydrogen 10-18 heme oxygenase 2 Homo sapiens 49-52 27465104-7 2016 abstracts hydrogen rapidly from H2 O2 to produce HO2 (.) Hydrogen Peroxide 32-37 heme oxygenase 2 Homo sapiens 49-52 27465104-13 2016 Hydroperoxyl radical (HO2 (.) Hydroperoxy radical 0-20 heme oxygenase 2 Homo sapiens 22-25 27531649-5 2016 CO generated by heme oxygenase-2 (HO-2) induces a signaling pathway that inhibits hydrogen sulfide (H2S) production by cystathionine gamma-lyase (CSE), leading to suppression of carotid body activity. Hydrogen Sulfide 82-98 heme oxygenase 2 Homo sapiens 16-32 27441526-2 2016 Using synchrotron-based time-resolved VUV photoionization mass spectrometry, we probe numerous transient intermediates and products at P = 10-2000 Torr and T = 400-700 K. A key reaction sequence, revealed by our experiments, is the conversion of THF-yl peroxy to hydroperoxy-THF-yl radicals (QOOH), followed by a second O2 addition and subsequent decomposition to dihydrofuranyl hydroperoxide + HO2 or to gamma-butyrolactone hydroperoxide + OH. thf-yl peroxy 246-259 heme oxygenase 2 Homo sapiens 395-398 27441526-2 2016 Using synchrotron-based time-resolved VUV photoionization mass spectrometry, we probe numerous transient intermediates and products at P = 10-2000 Torr and T = 400-700 K. A key reaction sequence, revealed by our experiments, is the conversion of THF-yl peroxy to hydroperoxy-THF-yl radicals (QOOH), followed by a second O2 addition and subsequent decomposition to dihydrofuranyl hydroperoxide + HO2 or to gamma-butyrolactone hydroperoxide + OH. hydroperoxy-thf-yl radicals 263-290 heme oxygenase 2 Homo sapiens 395-398 27441526-2 2016 Using synchrotron-based time-resolved VUV photoionization mass spectrometry, we probe numerous transient intermediates and products at P = 10-2000 Torr and T = 400-700 K. A key reaction sequence, revealed by our experiments, is the conversion of THF-yl peroxy to hydroperoxy-THF-yl radicals (QOOH), followed by a second O2 addition and subsequent decomposition to dihydrofuranyl hydroperoxide + HO2 or to gamma-butyrolactone hydroperoxide + OH. qooh 292-296 heme oxygenase 2 Homo sapiens 395-398 27441526-2 2016 Using synchrotron-based time-resolved VUV photoionization mass spectrometry, we probe numerous transient intermediates and products at P = 10-2000 Torr and T = 400-700 K. A key reaction sequence, revealed by our experiments, is the conversion of THF-yl peroxy to hydroperoxy-THF-yl radicals (QOOH), followed by a second O2 addition and subsequent decomposition to dihydrofuranyl hydroperoxide + HO2 or to gamma-butyrolactone hydroperoxide + OH. Oxygen 320-322 heme oxygenase 2 Homo sapiens 395-398 27441526-2 2016 Using synchrotron-based time-resolved VUV photoionization mass spectrometry, we probe numerous transient intermediates and products at P = 10-2000 Torr and T = 400-700 K. A key reaction sequence, revealed by our experiments, is the conversion of THF-yl peroxy to hydroperoxy-THF-yl radicals (QOOH), followed by a second O2 addition and subsequent decomposition to dihydrofuranyl hydroperoxide + HO2 or to gamma-butyrolactone hydroperoxide + OH. dihydrofuranyl hydroperoxide 364-392 heme oxygenase 2 Homo sapiens 395-398 27441526-2 2016 Using synchrotron-based time-resolved VUV photoionization mass spectrometry, we probe numerous transient intermediates and products at P = 10-2000 Torr and T = 400-700 K. A key reaction sequence, revealed by our experiments, is the conversion of THF-yl peroxy to hydroperoxy-THF-yl radicals (QOOH), followed by a second O2 addition and subsequent decomposition to dihydrofuranyl hydroperoxide + HO2 or to gamma-butyrolactone hydroperoxide + OH. gamma-butyrolactone hydroperoxide 405-438 heme oxygenase 2 Homo sapiens 395-398 27531649-9 2016 Thus, our results indicate that oxidant-induced inactivation of HO-2, which leads to increased CSE-dependent H2S production in the carotid body, is a critical trigger of hypertension in rodents exposed to intermittent hypoxia. Hydrogen Sulfide 109-112 heme oxygenase 2 Homo sapiens 64-68 27531649-5 2016 CO generated by heme oxygenase-2 (HO-2) induces a signaling pathway that inhibits hydrogen sulfide (H2S) production by cystathionine gamma-lyase (CSE), leading to suppression of carotid body activity. Hydrogen Sulfide 82-98 heme oxygenase 2 Homo sapiens 34-38 27531649-5 2016 CO generated by heme oxygenase-2 (HO-2) induces a signaling pathway that inhibits hydrogen sulfide (H2S) production by cystathionine gamma-lyase (CSE), leading to suppression of carotid body activity. Hydrogen Sulfide 100-103 heme oxygenase 2 Homo sapiens 16-32 27531649-5 2016 CO generated by heme oxygenase-2 (HO-2) induces a signaling pathway that inhibits hydrogen sulfide (H2S) production by cystathionine gamma-lyase (CSE), leading to suppression of carotid body activity. Hydrogen Sulfide 100-103 heme oxygenase 2 Homo sapiens 34-38 27531649-6 2016 We found that ROS inhibited CO generation by HO-2 in the carotid body and liver through a mechanism that required Cys(265) in the heme regulatory motif of heterologously expressed HO-2. Reactive Oxygen Species 14-17 heme oxygenase 2 Homo sapiens 45-49 27531649-6 2016 We found that ROS inhibited CO generation by HO-2 in the carotid body and liver through a mechanism that required Cys(265) in the heme regulatory motif of heterologously expressed HO-2. Reactive Oxygen Species 14-17 heme oxygenase 2 Homo sapiens 180-184 27531649-6 2016 We found that ROS inhibited CO generation by HO-2 in the carotid body and liver through a mechanism that required Cys(265) in the heme regulatory motif of heterologously expressed HO-2. Cysteine 114-117 heme oxygenase 2 Homo sapiens 45-49 27531649-6 2016 We found that ROS inhibited CO generation by HO-2 in the carotid body and liver through a mechanism that required Cys(265) in the heme regulatory motif of heterologously expressed HO-2. Cysteine 114-117 heme oxygenase 2 Homo sapiens 180-184 27531649-6 2016 We found that ROS inhibited CO generation by HO-2 in the carotid body and liver through a mechanism that required Cys(265) in the heme regulatory motif of heterologously expressed HO-2. Heme 130-134 heme oxygenase 2 Homo sapiens 45-49 27531649-6 2016 We found that ROS inhibited CO generation by HO-2 in the carotid body and liver through a mechanism that required Cys(265) in the heme regulatory motif of heterologously expressed HO-2. Heme 130-134 heme oxygenase 2 Homo sapiens 180-184 27254650-0 2016 The catalytic effect of water, water dimers and water trimers on H2S + (3)O2 formation by the HO2 + HS reaction under tropospheric conditions. Water 24-29 heme oxygenase 2 Homo sapiens 94-97 26955896-7 2016 HO2 ) for methylene blue degradation, which might account for their high catalytic activity. Methylene Blue 10-24 heme oxygenase 2 Homo sapiens 0-3 27397411-0 2016 Importance of Unimolecular HO2 Elimination in the Heterogeneous OH Reaction of Highly Oxygenated Tartaric Acid Aerosol. tartaric acid 97-110 heme oxygenase 2 Homo sapiens 27-30 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 42-47 heme oxygenase 2 Homo sapiens 207-210 27254650-0 2016 The catalytic effect of water, water dimers and water trimers on H2S + (3)O2 formation by the HO2 + HS reaction under tropospheric conditions. Water 31-36 heme oxygenase 2 Homo sapiens 94-97 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Hydrogen 197-199 heme oxygenase 2 Homo sapiens 188-191 27254650-0 2016 The catalytic effect of water, water dimers and water trimers on H2S + (3)O2 formation by the HO2 + HS reaction under tropospheric conditions. Water 31-36 heme oxygenase 2 Homo sapiens 94-97 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. h2oho2 204-210 heme oxygenase 2 Homo sapiens 188-191 27254650-0 2016 The catalytic effect of water, water dimers and water trimers on H2S + (3)O2 formation by the HO2 + HS reaction under tropospheric conditions. Hydrogen Sulfide 65-68 heme oxygenase 2 Homo sapiens 94-97 27254650-0 2016 The catalytic effect of water, water dimers and water trimers on H2S + (3)O2 formation by the HO2 + HS reaction under tropospheric conditions. (3)o2 71-76 heme oxygenase 2 Homo sapiens 94-97 27254650-1 2016 In this article, the reaction mechanisms of H2S + (3)O2 formation by the HO2 + HS reaction without and with catalyst X (X = H2O, (H2O)2 and (H2O)3) have been investigated theoretically at the CCSD(T)/6-311++G(3df,2pd)//B3LYP/6-311+G(2df,2p) level of theory, coupled with rate constant calculations by using conventional transition state theory. Hydrogen Sulfide 44-47 heme oxygenase 2 Homo sapiens 73-76 27254650-1 2016 In this article, the reaction mechanisms of H2S + (3)O2 formation by the HO2 + HS reaction without and with catalyst X (X = H2O, (H2O)2 and (H2O)3) have been investigated theoretically at the CCSD(T)/6-311++G(3df,2pd)//B3LYP/6-311+G(2df,2p) level of theory, coupled with rate constant calculations by using conventional transition state theory. (3)o2 50-55 heme oxygenase 2 Homo sapiens 73-76 27254650-1 2016 In this article, the reaction mechanisms of H2S + (3)O2 formation by the HO2 + HS reaction without and with catalyst X (X = H2O, (H2O)2 and (H2O)3) have been investigated theoretically at the CCSD(T)/6-311++G(3df,2pd)//B3LYP/6-311+G(2df,2p) level of theory, coupled with rate constant calculations by using conventional transition state theory. Hydrogen 79-81 heme oxygenase 2 Homo sapiens 73-76 27254650-1 2016 In this article, the reaction mechanisms of H2S + (3)O2 formation by the HO2 + HS reaction without and with catalyst X (X = H2O, (H2O)2 and (H2O)3) have been investigated theoretically at the CCSD(T)/6-311++G(3df,2pd)//B3LYP/6-311+G(2df,2p) level of theory, coupled with rate constant calculations by using conventional transition state theory. Water 124-127 heme oxygenase 2 Homo sapiens 73-76 27254650-1 2016 In this article, the reaction mechanisms of H2S + (3)O2 formation by the HO2 + HS reaction without and with catalyst X (X = H2O, (H2O)2 and (H2O)3) have been investigated theoretically at the CCSD(T)/6-311++G(3df,2pd)//B3LYP/6-311+G(2df,2p) level of theory, coupled with rate constant calculations by using conventional transition state theory. Water 130-133 heme oxygenase 2 Homo sapiens 73-76 27254650-1 2016 In this article, the reaction mechanisms of H2S + (3)O2 formation by the HO2 + HS reaction without and with catalyst X (X = H2O, (H2O)2 and (H2O)3) have been investigated theoretically at the CCSD(T)/6-311++G(3df,2pd)//B3LYP/6-311+G(2df,2p) level of theory, coupled with rate constant calculations by using conventional transition state theory. Water 130-133 heme oxygenase 2 Homo sapiens 73-76 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 35-40 heme oxygenase 2 Homo sapiens 188-191 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 35-40 heme oxygenase 2 Homo sapiens 207-210 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 42-47 heme oxygenase 2 Homo sapiens 188-191 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 42-47 heme oxygenase 2 Homo sapiens 207-210 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 42-47 heme oxygenase 2 Homo sapiens 188-191 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 42-47 heme oxygenase 2 Homo sapiens 207-210 27254650-3 2016 Meanwhile, the catalytic effect of water, water dimers and water trimers is mainly taken from the contribution of a single water vapor molecule, since the total effective rate constant of HO2H2O + HS and H2OHO2 + HS reactions was, respectively, larger by 7-9 and 9-12 orders of magnitude than that of SH + HO2(H2O)2 and SH + HO2(H2O)3 reactions. Water 42-47 heme oxygenase 2 Homo sapiens 188-191 27163880-0 2016 Unimolecular HO2 Loss from Peroxy Radicals Formed in Autoxidation Is Unlikely under Atmospheric Conditions. peroxy radicals 27-42 heme oxygenase 2 Homo sapiens 13-16 27163880-1 2016 A concerted HO2 loss reaction from a peroxy radical (RO2), formed from the addition of O2 to an alkyl radical, has been proposed as a mechanism to form closed-shell products in the atmospheric oxidation of organic molecules. Oxygen 37-51 heme oxygenase 2 Homo sapiens 12-15 27163880-1 2016 A concerted HO2 loss reaction from a peroxy radical (RO2), formed from the addition of O2 to an alkyl radical, has been proposed as a mechanism to form closed-shell products in the atmospheric oxidation of organic molecules. ro2 53-56 heme oxygenase 2 Homo sapiens 12-15 27163880-1 2016 A concerted HO2 loss reaction from a peroxy radical (RO2), formed from the addition of O2 to an alkyl radical, has been proposed as a mechanism to form closed-shell products in the atmospheric oxidation of organic molecules. alkyl radical 96-109 heme oxygenase 2 Homo sapiens 12-15 27164019-0 2016 Theoretical Prediction of Rate Constants for Hydrogen Abstraction by OH, H, O, CH3, and HO2 Radicals from Toluene. Hydrogen 45-53 heme oxygenase 2 Homo sapiens 88-91 27164019-0 2016 Theoretical Prediction of Rate Constants for Hydrogen Abstraction by OH, H, O, CH3, and HO2 Radicals from Toluene. Toluene 106-113 heme oxygenase 2 Homo sapiens 88-91 27164019-1 2016 Hydrogen abstraction from toluene by OH, H, O, CH3, and HO2 radicals are important reactions in oxidation process of toluene. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 56-59 27164019-1 2016 Hydrogen abstraction from toluene by OH, H, O, CH3, and HO2 radicals are important reactions in oxidation process of toluene. Toluene 26-33 heme oxygenase 2 Homo sapiens 56-59 27164019-1 2016 Hydrogen abstraction from toluene by OH, H, O, CH3, and HO2 radicals are important reactions in oxidation process of toluene. Toluene 117-124 heme oxygenase 2 Homo sapiens 56-59 27140863-3 2016 Very little HO2(+) is seen from the reaction of H3(+) with O2, which is attributed to an efficient secondary reaction between HO2(+) and H2. Oxygen 13-15 heme oxygenase 2 Homo sapiens 126-129 27140863-3 2016 Very little HO2(+) is seen from the reaction of H3(+) with O2, which is attributed to an efficient secondary reaction between HO2(+) and H2. Hydrogen 137-139 heme oxygenase 2 Homo sapiens 12-15 27140863-3 2016 Very little HO2(+) is seen from the reaction of H3(+) with O2, which is attributed to an efficient secondary reaction between HO2(+) and H2. Hydrogen 137-139 heme oxygenase 2 Homo sapiens 126-129 27033381-6 2016 The short-lived reactive oxygen species (ROS) and reactive nitrogen species (RNS) are strongly coupled in liquid-phase reactions: NO3 is an important precursor for short-lived ROS, and in turn OH, O2(-) and HO2 play a crucial role for the production of short-lived RNS. Reactive Oxygen Species 16-39 heme oxygenase 2 Homo sapiens 207-210 27826418-0 2016 Cysteine-independent activation/inhibition of heme oxygenase-2. Cysteine 0-8 heme oxygenase 2 Homo sapiens 46-62 27826418-2 2016 The heme oxygenase-2 (HO-2) isozyme contains two cys residues that have been implicated in binding of heme and also the regulation of its activity. Cysteine 49-52 heme oxygenase 2 Homo sapiens 4-20 27826418-2 2016 The heme oxygenase-2 (HO-2) isozyme contains two cys residues that have been implicated in binding of heme and also the regulation of its activity. Cysteine 49-52 heme oxygenase 2 Homo sapiens 22-26 27826418-2 2016 The heme oxygenase-2 (HO-2) isozyme contains two cys residues that have been implicated in binding of heme and also the regulation of its activity. Heme 4-8 heme oxygenase 2 Homo sapiens 22-26 27826418-3 2016 In this paper, we address the question of a role for cys residues for the HO-2 inhibitors or activators designed in our laboratory. Cysteine 53-56 heme oxygenase 2 Homo sapiens 74-78 27826418-4 2016 We tested the activity of full length recombinant human heme oxygenase-2 (FL-hHO-2) and its analog in which cys265 and cys282 were both replaced by alanine to determine the effect on activation by menadione (MD) and inhibition by QC-2350. Vitamin K 3 197-206 heme oxygenase 2 Homo sapiens 56-72 27826418-6 2016 Our findings are interpreted to mean that thiols of FL-hHO-2s are not involved in HO-2 activation or inhibition by the compounds that have been designed and identified by us. Sulfhydryl Compounds 42-48 heme oxygenase 2 Homo sapiens 56-60 27453774-3 2016 The addition of a spin trapping reagent resulted in formation of a spin adduct of hydroperoxyl radical (HO2 ), as observed by EPR spectroscopy, inhibiting phenol formation. Hydroperoxy radical 82-102 heme oxygenase 2 Homo sapiens 104-107 27453774-3 2016 The addition of a spin trapping reagent resulted in formation of a spin adduct of hydroperoxyl radical (HO2 ), as observed by EPR spectroscopy, inhibiting phenol formation. Phenol 155-161 heme oxygenase 2 Homo sapiens 104-107 27453774-4 2016 HO2 produced by the reaction of [Cu(tmpa)]2+ with H2O2 acts as a chain carrier for the radical chain reactions for formation of phenol. trimethyl phosphate 37-41 heme oxygenase 2 Homo sapiens 0-3 27453774-4 2016 HO2 produced by the reaction of [Cu(tmpa)]2+ with H2O2 acts as a chain carrier for the radical chain reactions for formation of phenol. Hydrogen Peroxide 51-55 heme oxygenase 2 Homo sapiens 0-3 27453774-4 2016 HO2 produced by the reaction of [Cu(tmpa)]2+ with H2O2 acts as a chain carrier for the radical chain reactions for formation of phenol. Phenol 129-135 heme oxygenase 2 Homo sapiens 0-3 27033381-6 2016 The short-lived reactive oxygen species (ROS) and reactive nitrogen species (RNS) are strongly coupled in liquid-phase reactions: NO3 is an important precursor for short-lived ROS, and in turn OH, O2(-) and HO2 play a crucial role for the production of short-lived RNS. Reactive Oxygen Species 41-44 heme oxygenase 2 Homo sapiens 207-210 27033381-6 2016 The short-lived reactive oxygen species (ROS) and reactive nitrogen species (RNS) are strongly coupled in liquid-phase reactions: NO3 is an important precursor for short-lived ROS, and in turn OH, O2(-) and HO2 play a crucial role for the production of short-lived RNS. Reactive Nitrogen Species 50-75 heme oxygenase 2 Homo sapiens 207-210 27033381-6 2016 The short-lived reactive oxygen species (ROS) and reactive nitrogen species (RNS) are strongly coupled in liquid-phase reactions: NO3 is an important precursor for short-lived ROS, and in turn OH, O2(-) and HO2 play a crucial role for the production of short-lived RNS. Reactive Nitrogen Species 77-80 heme oxygenase 2 Homo sapiens 207-210 27033381-6 2016 The short-lived reactive oxygen species (ROS) and reactive nitrogen species (RNS) are strongly coupled in liquid-phase reactions: NO3 is an important precursor for short-lived ROS, and in turn OH, O2(-) and HO2 play a crucial role for the production of short-lived RNS. Reactive Oxygen Species 176-179 heme oxygenase 2 Homo sapiens 207-210 27033381-6 2016 The short-lived reactive oxygen species (ROS) and reactive nitrogen species (RNS) are strongly coupled in liquid-phase reactions: NO3 is an important precursor for short-lived ROS, and in turn OH, O2(-) and HO2 play a crucial role for the production of short-lived RNS. Reactive Nitrogen Species 265-268 heme oxygenase 2 Homo sapiens 207-210 26484935-0 2016 Organics Substantially Reduce HO2 Uptake onto Aerosols Containing Transition Metal ions. Metals 77-82 heme oxygenase 2 Homo sapiens 30-33 27023525-1 2016 Carbon monoxide (CO) produced by heme oxygenase (HO)-1 and HO-2 or released from the CO-donor, tricarbonyldichlororuthenium (II) dimer (CORM-2) causes vasodilation, with unknown efficacy against stress-induced gastric lesions. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 59-63 27023525-1 2016 Carbon monoxide (CO) produced by heme oxygenase (HO)-1 and HO-2 or released from the CO-donor, tricarbonyldichlororuthenium (II) dimer (CORM-2) causes vasodilation, with unknown efficacy against stress-induced gastric lesions. Carbon Monoxide 17-19 heme oxygenase 2 Homo sapiens 59-63 27023525-1 2016 Carbon monoxide (CO) produced by heme oxygenase (HO)-1 and HO-2 or released from the CO-donor, tricarbonyldichlororuthenium (II) dimer (CORM-2) causes vasodilation, with unknown efficacy against stress-induced gastric lesions. tricarbonyldichlororuthenium 95-123 heme oxygenase 2 Homo sapiens 59-63 26910881-0 2016 Low Temperature Chlorine-Initiated Oxidation of Small-Chain Methyl Esters: Quantification of Chain-Terminating HO2-Elimination Channels. Chlorine 16-24 heme oxygenase 2 Homo sapiens 111-114 26910881-0 2016 Low Temperature Chlorine-Initiated Oxidation of Small-Chain Methyl Esters: Quantification of Chain-Terminating HO2-Elimination Channels. methyl esters 60-73 heme oxygenase 2 Homo sapiens 111-114 26910881-3 2016 In each case, after addition of O2 to the initial radicals, chain-terminating HO2-elimination reactions are observed to be important. Oxygen 32-34 heme oxygenase 2 Homo sapiens 78-81 26910881-4 2016 Branching ratios among competing HO2-elimination channels are determined via absolute photoionization spectra of the unsaturated methyl ester coproducts. unsaturated methyl ester 117-141 heme oxygenase 2 Homo sapiens 33-36 26910881-5 2016 At 550 K, HO2-elimination is observed to be selective, resulting in nearly exclusive production of the conjugated methyl ester coproducts, methyl propenoate, methyl-2-butenoate, and methyl-2-pentenoate, respectively. methyl ester 114-126 heme oxygenase 2 Homo sapiens 10-13 26910881-5 2016 At 550 K, HO2-elimination is observed to be selective, resulting in nearly exclusive production of the conjugated methyl ester coproducts, methyl propenoate, methyl-2-butenoate, and methyl-2-pentenoate, respectively. methyl acrylate 139-156 heme oxygenase 2 Homo sapiens 10-13 26910881-5 2016 At 550 K, HO2-elimination is observed to be selective, resulting in nearly exclusive production of the conjugated methyl ester coproducts, methyl propenoate, methyl-2-butenoate, and methyl-2-pentenoate, respectively. methyl-2-butenoate 158-176 heme oxygenase 2 Homo sapiens 10-13 26910881-5 2016 At 550 K, HO2-elimination is observed to be selective, resulting in nearly exclusive production of the conjugated methyl ester coproducts, methyl propenoate, methyl-2-butenoate, and methyl-2-pentenoate, respectively. Methyl 2-pentenoate 182-201 heme oxygenase 2 Homo sapiens 10-13 26910881-6 2016 However, in MV, upon raising the temperature to 650 K, other HO2-elimination pathways are observed that yield methyl-3-pentenoate and methyl-4-pentenoate. methyl-3 penteneoate 110-129 heme oxygenase 2 Homo sapiens 61-64 26910881-6 2016 However, in MV, upon raising the temperature to 650 K, other HO2-elimination pathways are observed that yield methyl-3-pentenoate and methyl-4-pentenoate. methyl pent-4-enoate 134-153 heme oxygenase 2 Homo sapiens 61-64 26484935-1 2016 A HO2 mass accommodation coefficient of alpha = 0.23 +- 0.07 was measured onto submicron copper(II)-doped ammonium sulfate aerosols at a relative humidity of 60 +- 3%, at 293 +- 2 K and at an initial HO2 concentration of ~ 1 x 10(9) molecules cm(-3) by using an aerosol flow tube coupled to a sensitive fluorescence assay by gas expansion (FAGE) HO2 detection system. cupric ion 89-99 heme oxygenase 2 Homo sapiens 2-5 26484935-1 2016 A HO2 mass accommodation coefficient of alpha = 0.23 +- 0.07 was measured onto submicron copper(II)-doped ammonium sulfate aerosols at a relative humidity of 60 +- 3%, at 293 +- 2 K and at an initial HO2 concentration of ~ 1 x 10(9) molecules cm(-3) by using an aerosol flow tube coupled to a sensitive fluorescence assay by gas expansion (FAGE) HO2 detection system. Ammonium Sulfate 106-122 heme oxygenase 2 Homo sapiens 2-5 26484935-2 2016 The effect upon the HO2 uptake coefficient gamma of adding different organic species (malonic acid, citric acid, 1,2-diaminoethane, tartronic acid, ethylenediaminetetraacetic acid (EDTA), and oxalic acid) into the copper(II)-doped aerosols was investigated. malonic acid 86-98 heme oxygenase 2 Homo sapiens 20-23 26484935-2 2016 The effect upon the HO2 uptake coefficient gamma of adding different organic species (malonic acid, citric acid, 1,2-diaminoethane, tartronic acid, ethylenediaminetetraacetic acid (EDTA), and oxalic acid) into the copper(II)-doped aerosols was investigated. ethylenediamine 113-130 heme oxygenase 2 Homo sapiens 20-23 26484935-2 2016 The effect upon the HO2 uptake coefficient gamma of adding different organic species (malonic acid, citric acid, 1,2-diaminoethane, tartronic acid, ethylenediaminetetraacetic acid (EDTA), and oxalic acid) into the copper(II)-doped aerosols was investigated. Edetic Acid 148-179 heme oxygenase 2 Homo sapiens 20-23 26484935-2 2016 The effect upon the HO2 uptake coefficient gamma of adding different organic species (malonic acid, citric acid, 1,2-diaminoethane, tartronic acid, ethylenediaminetetraacetic acid (EDTA), and oxalic acid) into the copper(II)-doped aerosols was investigated. Edetic Acid 181-185 heme oxygenase 2 Homo sapiens 20-23 26484935-2 2016 The effect upon the HO2 uptake coefficient gamma of adding different organic species (malonic acid, citric acid, 1,2-diaminoethane, tartronic acid, ethylenediaminetetraacetic acid (EDTA), and oxalic acid) into the copper(II)-doped aerosols was investigated. Oxalic Acid 192-203 heme oxygenase 2 Homo sapiens 20-23 26484935-2 2016 The effect upon the HO2 uptake coefficient gamma of adding different organic species (malonic acid, citric acid, 1,2-diaminoethane, tartronic acid, ethylenediaminetetraacetic acid (EDTA), and oxalic acid) into the copper(II)-doped aerosols was investigated. cupric ion 214-224 heme oxygenase 2 Homo sapiens 20-23 26484935-2 2016 The effect upon the HO2 uptake coefficient gamma of adding different organic species (malonic acid, citric acid, 1,2-diaminoethane, tartronic acid, ethylenediaminetetraacetic acid (EDTA), and oxalic acid) into the copper(II)-doped aerosols was investigated. doped 225-230 heme oxygenase 2 Homo sapiens 20-23 26484935-3 2016 The HO2 uptake coefficient decreased steadily from the mass accommodation value to gamma = 0.008 +- 0.009 when EDTA was added in a one-to-one molar ratio with the copper(II) ions, and to gamma = 0.003 +- 0.004 when oxalic acid was added into the aerosol in a ten-to-one molar ratio with the copper(II). Edetic Acid 111-115 heme oxygenase 2 Homo sapiens 4-7 26484935-3 2016 The HO2 uptake coefficient decreased steadily from the mass accommodation value to gamma = 0.008 +- 0.009 when EDTA was added in a one-to-one molar ratio with the copper(II) ions, and to gamma = 0.003 +- 0.004 when oxalic acid was added into the aerosol in a ten-to-one molar ratio with the copper(II). Copper 163-169 heme oxygenase 2 Homo sapiens 4-7 26484935-3 2016 The HO2 uptake coefficient decreased steadily from the mass accommodation value to gamma = 0.008 +- 0.009 when EDTA was added in a one-to-one molar ratio with the copper(II) ions, and to gamma = 0.003 +- 0.004 when oxalic acid was added into the aerosol in a ten-to-one molar ratio with the copper(II). Oxalic Acid 215-226 heme oxygenase 2 Homo sapiens 4-7 26484935-3 2016 The HO2 uptake coefficient decreased steadily from the mass accommodation value to gamma = 0.008 +- 0.009 when EDTA was added in a one-to-one molar ratio with the copper(II) ions, and to gamma = 0.003 +- 0.004 when oxalic acid was added into the aerosol in a ten-to-one molar ratio with the copper(II). Copper 291-297 heme oxygenase 2 Homo sapiens 4-7 26484935-4 2016 EDTA binds strongly to copper(II) ions, potentially making them unavailable for catalytic destruction of HO2, and could also be acting as a surfactant or changing the viscosity of the aerosol. Edetic Acid 0-4 heme oxygenase 2 Homo sapiens 105-108 26484935-5 2016 The addition of oxalic acid to the aerosol potentially forms low-volatility copper-oxalate complexes that reduce the uptake of HO2 either by changing the viscosity of the aerosol or by causing precipitation out of the aerosol forming a coating. Oxalic Acid 16-27 heme oxygenase 2 Homo sapiens 127-130 26484935-5 2016 The addition of oxalic acid to the aerosol potentially forms low-volatility copper-oxalate complexes that reduce the uptake of HO2 either by changing the viscosity of the aerosol or by causing precipitation out of the aerosol forming a coating. Copper oxalate 76-90 heme oxygenase 2 Homo sapiens 127-130 26484935-6 2016 It is likely that there is a high enough oxalate to copper(II) ion ratio in many types of atmospheric aerosols to decrease the HO2 uptake coefficient. Oxalates 41-48 heme oxygenase 2 Homo sapiens 127-130 26484935-6 2016 It is likely that there is a high enough oxalate to copper(II) ion ratio in many types of atmospheric aerosols to decrease the HO2 uptake coefficient. cupric ion 52-62 heme oxygenase 2 Homo sapiens 127-130 26575342-1 2016 NOx (NOx NO + NO2) regulates O3 and HOx (HOx OH + HO2) concentrations in the upper troposphere. nicotine 1-N-oxide 0-3 heme oxygenase 2 Homo sapiens 54-57 26575342-1 2016 NOx (NOx NO + NO2) regulates O3 and HOx (HOx OH + HO2) concentrations in the upper troposphere. nox no 5-13 heme oxygenase 2 Homo sapiens 54-57 26575342-1 2016 NOx (NOx NO + NO2) regulates O3 and HOx (HOx OH + HO2) concentrations in the upper troposphere. Nitrogen Dioxide 16-19 heme oxygenase 2 Homo sapiens 54-57 26575342-1 2016 NOx (NOx NO + NO2) regulates O3 and HOx (HOx OH + HO2) concentrations in the upper troposphere. hydrogen oxalate 38-41 heme oxygenase 2 Homo sapiens 54-57 26575342-7 2016 The analysis indicates that HNO3 production from the HO2 and NO reaction (if any) must be accompanied by a slower rate for the reaction of OH with NO2, keeping the total combined rate for the two processes at the rate reported for HNO3 production above. Nitric Acid 28-32 heme oxygenase 2 Homo sapiens 53-56 26575342-7 2016 The analysis indicates that HNO3 production from the HO2 and NO reaction (if any) must be accompanied by a slower rate for the reaction of OH with NO2, keeping the total combined rate for the two processes at the rate reported for HNO3 production above. Nitrogen Dioxide 147-150 heme oxygenase 2 Homo sapiens 53-56 26575342-7 2016 The analysis indicates that HNO3 production from the HO2 and NO reaction (if any) must be accompanied by a slower rate for the reaction of OH with NO2, keeping the total combined rate for the two processes at the rate reported for HNO3 production above. Nitric Acid 231-235 heme oxygenase 2 Homo sapiens 53-56 26530893-8 2016 The mechanisms of the photocatalytic coagulation oxidation of Ti(SO4)2 are similar to those of UV/crystalline TiO2 particles, involving the formation and reactions of the hydroxyl radical OH and superoxide HO2/O2(-). Titanium(IV) sulfate 62-70 heme oxygenase 2 Homo sapiens 206-209 26853854-4 2016 Addition of hydroperoxy radical precursors to the gas mixture (methanol and oxygen) subsequently led to a competition for photolytically generated Cl atoms and a simultaneous prompt formation of both ClO and HO2 radicals. perhydroxyl radical 12-31 heme oxygenase 2 Homo sapiens 208-211 26853854-4 2016 Addition of hydroperoxy radical precursors to the gas mixture (methanol and oxygen) subsequently led to a competition for photolytically generated Cl atoms and a simultaneous prompt formation of both ClO and HO2 radicals. Methanol 63-71 heme oxygenase 2 Homo sapiens 208-211 26853854-4 2016 Addition of hydroperoxy radical precursors to the gas mixture (methanol and oxygen) subsequently led to a competition for photolytically generated Cl atoms and a simultaneous prompt formation of both ClO and HO2 radicals. Oxygen 76-82 heme oxygenase 2 Homo sapiens 208-211 26830670-5 2016 Under the chosen reaction conditions, product formation was dominated by highly oxidized RO2 radicals which react with NO, NO2, HO2, and other RO2 radicals under atmospheric conditions. ro2 radicals 89-101 heme oxygenase 2 Homo sapiens 128-131 26530893-8 2016 The mechanisms of the photocatalytic coagulation oxidation of Ti(SO4)2 are similar to those of UV/crystalline TiO2 particles, involving the formation and reactions of the hydroxyl radical OH and superoxide HO2/O2(-). titanium dioxide 110-114 heme oxygenase 2 Homo sapiens 206-209 26530893-8 2016 The mechanisms of the photocatalytic coagulation oxidation of Ti(SO4)2 are similar to those of UV/crystalline TiO2 particles, involving the formation and reactions of the hydroxyl radical OH and superoxide HO2/O2(-). Superoxides 195-205 heme oxygenase 2 Homo sapiens 206-209 26530893-8 2016 The mechanisms of the photocatalytic coagulation oxidation of Ti(SO4)2 are similar to those of UV/crystalline TiO2 particles, involving the formation and reactions of the hydroxyl radical OH and superoxide HO2/O2(-). Superoxides 112-114 heme oxygenase 2 Homo sapiens 206-209 26652036-6 2016 Furthermore, heme hydroxylation proceeds three times more slowly, and the oxy-Fe(II) state is 100-fold less stable in HO2 than in HO1. oxy-fe(ii) 74-84 heme oxygenase 2 Homo sapiens 118-121 26652036-1 2016 The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Heme 26-30 heme oxygenase 2 Homo sapiens 50-53 26652036-1 2016 The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Biliverdine 97-107 heme oxygenase 2 Homo sapiens 50-53 26652036-1 2016 The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Iron 109-111 heme oxygenase 2 Homo sapiens 50-53 26652036-1 2016 The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Carbon Monoxide 117-119 heme oxygenase 2 Homo sapiens 50-53 26652036-2 2016 Unlike HO1, HO2 contains two C-terminal heme regulatory motifs (HRMs) centered at Cys265 and Cys282 that act as redox switches and, in their reduced dithiolate state, bind heme (Fleischhacker et al., Biochemistry , 2015 , 54 , 2693 - 2708 ). Heme 40-44 heme oxygenase 2 Homo sapiens 12-15 26652036-2 2016 Unlike HO1, HO2 contains two C-terminal heme regulatory motifs (HRMs) centered at Cys265 and Cys282 that act as redox switches and, in their reduced dithiolate state, bind heme (Fleischhacker et al., Biochemistry , 2015 , 54 , 2693 - 2708 ). dithiolate 149-159 heme oxygenase 2 Homo sapiens 12-15 26652036-2 2016 Unlike HO1, HO2 contains two C-terminal heme regulatory motifs (HRMs) centered at Cys265 and Cys282 that act as redox switches and, in their reduced dithiolate state, bind heme (Fleischhacker et al., Biochemistry , 2015 , 54 , 2693 - 2708 ). Heme 172-176 heme oxygenase 2 Homo sapiens 12-15 26652036-3 2016 Here, we describe cryoreduction/annealing and electron paramagnetic resonance spectroscopic experiments to study the structural features of the oxyheme moiety in HO2 and to elucidate the initial steps in heme degradation. oxyheme 144-151 heme oxygenase 2 Homo sapiens 162-165 26781569-8 2016 Furthermore, our in vitro experiments indicated that the C allele of rs4786504 could increase the expression of HMOX2, presumably leading to a more efficient breakdown of heme that may help maintain a relatively low hemoglobin level at high altitude. Heme 171-175 heme oxygenase 2 Homo sapiens 112-117 26658549-0 2016 Path-dependent variational effects and multidimensional tunneling in multi-path variational transition state theory: rate constants calculated for the reactions of HO2 with tert-butanol by including all 46 paths for abstraction at C and all six paths for abstraction at O. Multi-path variational transition state theory (MP-VTST) provides a conformationally complete framework for calculating gas-phase rate constants. tert-Butyl Alcohol 173-185 heme oxygenase 2 Homo sapiens 164-167 26658549-3 2016 In this work, we present calculations including all paths for two prototype combustion reactions, namely the two hydrogen abstraction reactions from tert-butanol by HO2 radical. Hydrogen 113-121 heme oxygenase 2 Homo sapiens 165-168 26658549-3 2016 In this work, we present calculations including all paths for two prototype combustion reactions, namely the two hydrogen abstraction reactions from tert-butanol by HO2 radical. tert-Butyl Alcohol 149-161 heme oxygenase 2 Homo sapiens 165-168 26652036-3 2016 Here, we describe cryoreduction/annealing and electron paramagnetic resonance spectroscopic experiments to study the structural features of the oxyheme moiety in HO2 and to elucidate the initial steps in heme degradation. Heme 147-151 heme oxygenase 2 Homo sapiens 162-165 26652036-8 2016 Kinetic studies revealed that heme oxygenation by HO2 occurs solely at the catalytic core in that a variant of HO2 lacking the C-terminal HRM domain exhibits the same specific activity as one containing both the catalytic core and HRM domain; furthermore, a truncated variant containing only the HRM region binds but cannot oxidize heme. Heme 30-34 heme oxygenase 2 Homo sapiens 50-53 26652036-8 2016 Kinetic studies revealed that heme oxygenation by HO2 occurs solely at the catalytic core in that a variant of HO2 lacking the C-terminal HRM domain exhibits the same specific activity as one containing both the catalytic core and HRM domain; furthermore, a truncated variant containing only the HRM region binds but cannot oxidize heme. Heme 30-34 heme oxygenase 2 Homo sapiens 111-114 26652036-8 2016 Kinetic studies revealed that heme oxygenation by HO2 occurs solely at the catalytic core in that a variant of HO2 lacking the C-terminal HRM domain exhibits the same specific activity as one containing both the catalytic core and HRM domain; furthermore, a truncated variant containing only the HRM region binds but cannot oxidize heme. Heme 332-336 heme oxygenase 2 Homo sapiens 50-53 26652036-8 2016 Kinetic studies revealed that heme oxygenation by HO2 occurs solely at the catalytic core in that a variant of HO2 lacking the C-terminal HRM domain exhibits the same specific activity as one containing both the catalytic core and HRM domain; furthermore, a truncated variant containing only the HRM region binds but cannot oxidize heme. Heme 332-336 heme oxygenase 2 Homo sapiens 111-114 26077317-10 2015 The key subsequent processes are the reactions Cl2(-) + O3 ClO + O2 + Cl(-) and ClO + H2O2 HOCl + HO2. Chlorine 47-53 heme oxygenase 2 Homo sapiens 102-105 26194238-8 2016 Scavenging experiments revealed that natural montmorillonite induced the conversion of As(III) to As(V) by generating ROS (mainly HO( ) and HO2( )/O2( -)) and that HO( ) radical was the predominant oxidant in this system. Bentonite 45-60 heme oxygenase 2 Homo sapiens 140-143 26194238-8 2016 Scavenging experiments revealed that natural montmorillonite induced the conversion of As(III) to As(V) by generating ROS (mainly HO( ) and HO2( )/O2( -)) and that HO( ) radical was the predominant oxidant in this system. as(iii) 87-94 heme oxygenase 2 Homo sapiens 140-143 26608471-3 2015 The photolysis of 2,3-pentanedione (PTD) has been investigated for the first time as a function of pressure in a static reactor equipped with continuous wave cavity ring-down spectroscopy to measure the HO2 radical photostationary concentrations along with stable species. 2,3-pentanedione 18-34 heme oxygenase 2 Homo sapiens 203-206 26608471-3 2015 The photolysis of 2,3-pentanedione (PTD) has been investigated for the first time as a function of pressure in a static reactor equipped with continuous wave cavity ring-down spectroscopy to measure the HO2 radical photostationary concentrations along with stable species. 2,3-pentanedione 36-39 heme oxygenase 2 Homo sapiens 203-206 26608471-6 2015 As a part of this work, the O2 broadening coefficient for the absorption line of HO2 radicals at 6638.21 cm(-1) has been determined (gammaO2 = 0.0289 cm(-1) atm(-1)). Oxygen 28-30 heme oxygenase 2 Homo sapiens 81-84 26555823-0 2015 Red-Light-Induced Decomposition of an Organic Peroxy Radical: A New Source of the HO2 Radical. Oxygen 46-60 heme oxygenase 2 Homo sapiens 82-85 26555823-1 2015 The gas-phase decomposition of the alpha-hydroxy methylperoxy radical has been theoretically examined, and the results provide insight into a new source of the hydroperoxy radical (HO2 ) in the troposphere. alpha-hydroxy methylperoxy radical 35-69 heme oxygenase 2 Homo sapiens 181-184 26555823-1 2015 The gas-phase decomposition of the alpha-hydroxy methylperoxy radical has been theoretically examined, and the results provide insight into a new source of the hydroperoxy radical (HO2 ) in the troposphere. perhydroxyl radical 160-179 heme oxygenase 2 Homo sapiens 181-184 26555823-4 2015 In particular, the reaction of organic peroxy radicals with the HO2 radical and the H2 O HO2 radical complex represent an autocatalytic source of atmospheric HO2 . peroxy radicals 39-54 heme oxygenase 2 Homo sapiens 64-67 26555823-4 2015 In particular, the reaction of organic peroxy radicals with the HO2 radical and the H2 O HO2 radical complex represent an autocatalytic source of atmospheric HO2 . peroxy radicals 39-54 heme oxygenase 2 Homo sapiens 89-92 26555823-4 2015 In particular, the reaction of organic peroxy radicals with the HO2 radical and the H2 O HO2 radical complex represent an autocatalytic source of atmospheric HO2 . peroxy radicals 39-54 heme oxygenase 2 Homo sapiens 89-92 26555823-4 2015 In particular, the reaction of organic peroxy radicals with the HO2 radical and the H2 O HO2 radical complex represent an autocatalytic source of atmospheric HO2 . Water 84-88 heme oxygenase 2 Homo sapiens 89-92 26555823-4 2015 In particular, the reaction of organic peroxy radicals with the HO2 radical and the H2 O HO2 radical complex represent an autocatalytic source of atmospheric HO2 . Water 84-88 heme oxygenase 2 Homo sapiens 89-92 30090268-3 2015 The rate-determining step in the catalytic cycle is hydrogen atom transfer from H3Trip to O2 in the H3Trip/O2 complex to produce the radical pair (H3Trip + HO2 ) as an intermediate, which was detected as a triplet EPR signal with fine-structure by the EPR measurements at low temperature. Hydrogen 52-60 heme oxygenase 2 Homo sapiens 156-159 30090268-3 2015 The rate-determining step in the catalytic cycle is hydrogen atom transfer from H3Trip to O2 in the H3Trip/O2 complex to produce the radical pair (H3Trip + HO2 ) as an intermediate, which was detected as a triplet EPR signal with fine-structure by the EPR measurements at low temperature. Oxygen 90-92 heme oxygenase 2 Homo sapiens 156-159 26077317-10 2015 The key subsequent processes are the reactions Cl2(-) + O3 ClO + O2 + Cl(-) and ClO + H2O2 HOCl + HO2. o3 clo 56-64 heme oxygenase 2 Homo sapiens 102-105 26077317-10 2015 The key subsequent processes are the reactions Cl2(-) + O3 ClO + O2 + Cl(-) and ClO + H2O2 HOCl + HO2. Oxygen 67-69 heme oxygenase 2 Homo sapiens 102-105 26077317-10 2015 The key subsequent processes are the reactions Cl2(-) + O3 ClO + O2 + Cl(-) and ClO + H2O2 HOCl + HO2. Hypochlorous Acid 61-64 heme oxygenase 2 Homo sapiens 102-105 26077317-10 2015 The key subsequent processes are the reactions Cl2(-) + O3 ClO + O2 + Cl(-) and ClO + H2O2 HOCl + HO2. Hydrogen Peroxide 88-92 heme oxygenase 2 Homo sapiens 102-105 26077317-10 2015 The key subsequent processes are the reactions Cl2(-) + O3 ClO + O2 + Cl(-) and ClO + H2O2 HOCl + HO2. Hypochlorous Acid 95-99 heme oxygenase 2 Homo sapiens 102-105 25860187-3 2015 At all three temperatures, the major stable product species is propene, formed in the propyl + O2 reactions by direct HO2 elimination from both n- and i-propyl peroxy radicals. propylene 63-70 heme oxygenase 2 Homo sapiens 118-121 26083133-0 2015 Structure-Activity Relationships of 1,2-Disubstituted Benzimidazoles: Selective Inhibition of Heme Oxygenase-2 Activity. 1,2-disubstituted benzimidazoles 36-68 heme oxygenase 2 Homo sapiens 94-110 26083133-2 2015 With a view of obtaining compounds that exhibit high potency and selectivity as inhibitors of the heme oxygenase-2 (HO-2) isozyme (constitutive) relative to the heme oxygenase-1 (HO-1) isozyme (inducible), several 1,2-disubstituted 1H-benzimidazoles were designed and synthesized. 1,2-disubstituted 1h-benzimidazoles 214-249 heme oxygenase 2 Homo sapiens 116-120 25611518-5 2015 An improved analytical representation of the temperature and pressure dependence of the rate constant is given for conditions where the chemical activation process C2H5 + O2 (+ M) C2H4 + HO2 (+ M) is only of minor importance. ethylene 182-186 heme oxygenase 2 Homo sapiens 189-192 26101896-6 2015 The process prevented Cu(2+) from oxidizing H2O2 to form HO2( )/O2( -) or O2, and enhanced the Cu(+)/Cu(2+) cycle, the formation of ( )OH, and the utilization efficiency of H2O2. cupric ion 22-28 heme oxygenase 2 Homo sapiens 57-60 26101896-6 2015 The process prevented Cu(2+) from oxidizing H2O2 to form HO2( )/O2( -) or O2, and enhanced the Cu(+)/Cu(2+) cycle, the formation of ( )OH, and the utilization efficiency of H2O2. Hydrogen Peroxide 44-48 heme oxygenase 2 Homo sapiens 57-60 26101896-6 2015 The process prevented Cu(2+) from oxidizing H2O2 to form HO2( )/O2( -) or O2, and enhanced the Cu(+)/Cu(2+) cycle, the formation of ( )OH, and the utilization efficiency of H2O2. Oxygen 46-48 heme oxygenase 2 Homo sapiens 57-60 26101896-6 2015 The process prevented Cu(2+) from oxidizing H2O2 to form HO2( )/O2( -) or O2, and enhanced the Cu(+)/Cu(2+) cycle, the formation of ( )OH, and the utilization efficiency of H2O2. Copper 22-24 heme oxygenase 2 Homo sapiens 57-60 25611968-0 2015 Glyoxal Oxidation Mechanism: Implications for the Reactions HCO + O2 and OCHCHO + HO2. Glyoxal 0-7 heme oxygenase 2 Homo sapiens 82-85 25860187-3 2015 At all three temperatures, the major stable product species is propene, formed in the propyl + O2 reactions by direct HO2 elimination from both n- and i-propyl peroxy radicals. Oxygen 95-97 heme oxygenase 2 Homo sapiens 118-121 25611968-5 2015 The temperature range of available direct rate constant data of the high-temperature key reaction HCO + O2 CO + HO2 has been extended up to 1705 K and confirms a temperature dependence consistent with a dominating direct abstraction channel. 7 alpha-hydroxy-4-cholesten-3-one 98-101 heme oxygenase 2 Homo sapiens 114-117 25611968-5 2015 The temperature range of available direct rate constant data of the high-temperature key reaction HCO + O2 CO + HO2 has been extended up to 1705 K and confirms a temperature dependence consistent with a dominating direct abstraction channel. Oxygen 104-106 heme oxygenase 2 Homo sapiens 114-117 25870904-10 2015 The kinetic analysis of the model enabled the highlighting of some specificities of the oxidation chemistry of DME: (1) the early reactivity which is observed at very low-temperature (e.g., compared to propane) is explained by the absence of inhibiting reaction of the radical directly obtained from the fuel (by H atom abstraction) with oxygen yielding an olefin + HO2 ; (2) the low-temperature reactivity is driven by the relative importance of the second addition to O2 (promoting the reactivity through branching chain) and the competitive decomposition reactions with an inhibiting effect. dimethyl ether 111-114 heme oxygenase 2 Homo sapiens 366-369 25860187-3 2015 At all three temperatures, the major stable product species is propene, formed in the propyl + O2 reactions by direct HO2 elimination from both n- and i-propyl peroxy radicals. n- and i-propyl peroxy radicals 144-175 heme oxygenase 2 Homo sapiens 118-121 26066551-1 2015 Self-reaction is an important sink for the hydroperoxy radical (HO2) in the atmosphere. perhydroxyl radical 43-62 heme oxygenase 2 Homo sapiens 64-67 26066551-4 2015 A, 2009, 113 (2), 499-506) that the minor product hydrogen tetroxide (HO4H) may act as a reservoir of HO2. hydrogen tetroxide 50-68 heme oxygenase 2 Homo sapiens 102-105 26066551-4 2015 A, 2009, 113 (2), 499-506) that the minor product hydrogen tetroxide (HO4H) may act as a reservoir of HO2. ho4h 70-74 heme oxygenase 2 Homo sapiens 102-105 26066551-5 2015 Here, we compute the thermochemistry of HO2 self-reactions to determine if either HO4H or the cyclic hydrogen-bound dimer (HO2)2 can act as reservoirs. ho4h 82-86 heme oxygenase 2 Homo sapiens 40-43 26066551-5 2015 Here, we compute the thermochemistry of HO2 self-reactions to determine if either HO4H or the cyclic hydrogen-bound dimer (HO2)2 can act as reservoirs. cyclic hydrogen 94-109 heme oxygenase 2 Homo sapiens 40-43 26066551-5 2015 Here, we compute the thermochemistry of HO2 self-reactions to determine if either HO4H or the cyclic hydrogen-bound dimer (HO2)2 can act as reservoirs. cyclic hydrogen 94-109 heme oxygenase 2 Homo sapiens 123-126 26066551-9 2015 Under conditions used in laboratory experiments ([HO2] > 10(12) molecules per cm(3), 220 K), H2O4 formation may be significant. h2o4 96-100 heme oxygenase 2 Homo sapiens 50-53 26032909-0 2015 Nitrogen and fluorine dual-doped mesoporous graphene: a high-performance metal-free ORR electrocatalyst with a super-low HO2(-) yield. Nitrogen 0-8 heme oxygenase 2 Homo sapiens 121-124 26032909-0 2015 Nitrogen and fluorine dual-doped mesoporous graphene: a high-performance metal-free ORR electrocatalyst with a super-low HO2(-) yield. Graphite 44-52 heme oxygenase 2 Homo sapiens 121-124 25974050-1 2015 The kinetics of hydrogen abstraction by five radicals (H, O((3)P), OH, CH3, and HO2) from methyl acetate (MA) is investigated theoretically in order to gain further understanding of certain aspects of the combustion chemistry of biodiesels, such as the effect of the ester moiety. Hydrogen 16-24 heme oxygenase 2 Homo sapiens 80-83 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Nitrogen Dioxide 124-127 heme oxygenase 2 Homo sapiens 149-164 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Nitrogen Dioxide 141-144 heme oxygenase 2 Homo sapiens 118-121 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Nitrogen Dioxide 141-144 heme oxygenase 2 Homo sapiens 129-132 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Nitrogen Dioxide 141-144 heme oxygenase 2 Homo sapiens 149-164 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 191-196 heme oxygenase 2 Homo sapiens 118-121 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 191-196 heme oxygenase 2 Homo sapiens 129-132 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 191-196 heme oxygenase 2 Homo sapiens 149-164 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 31-34 heme oxygenase 2 Homo sapiens 37-40 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 31-34 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 31-34 heme oxygenase 2 Homo sapiens 182-185 25988324-0 2015 Can a single water molecule really affect the HO2 + NO2 hydrogen abstraction reaction under tropospheric conditions? Water 13-18 heme oxygenase 2 Homo sapiens 46-49 25988324-0 2015 Can a single water molecule really affect the HO2 + NO2 hydrogen abstraction reaction under tropospheric conditions? Nitrogen Dioxide 52-55 heme oxygenase 2 Homo sapiens 46-49 25988324-0 2015 Can a single water molecule really affect the HO2 + NO2 hydrogen abstraction reaction under tropospheric conditions? Hydrogen 56-64 heme oxygenase 2 Homo sapiens 46-49 25988324-1 2015 The effect of a single water molecule on the HO2 + NO2 hydrogen abstraction reaction has been investigated by employing B3LYP and CCSD(T) theoretical approaches with the aug-cc-pVTZ basis set. Water 23-28 heme oxygenase 2 Homo sapiens 45-48 25988324-1 2015 The effect of a single water molecule on the HO2 + NO2 hydrogen abstraction reaction has been investigated by employing B3LYP and CCSD(T) theoretical approaches with the aug-cc-pVTZ basis set. Hydrogen 55-63 heme oxygenase 2 Homo sapiens 45-48 25988324-2 2015 The reaction without water has three types of reaction channels on both singlet and triplet potential energy surfaces, depending on how the HO2 radical approaches NO2. Water 21-26 heme oxygenase 2 Homo sapiens 140-143 25988324-2 2015 The reaction without water has three types of reaction channels on both singlet and triplet potential energy surfaces, depending on how the HO2 radical approaches NO2. Nitrogen Dioxide 163-166 heme oxygenase 2 Homo sapiens 140-143 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 9-14 heme oxygenase 2 Homo sapiens 118-121 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 9-14 heme oxygenase 2 Homo sapiens 129-132 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 9-14 heme oxygenase 2 Homo sapiens 149-164 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 112-115 heme oxygenase 2 Homo sapiens 118-121 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 112-115 heme oxygenase 2 Homo sapiens 129-132 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Water 112-115 heme oxygenase 2 Homo sapiens 149-164 25988324-5 2015 A single water molecule affects each one of these triplet reaction channels in the three different reactions of H2O HO2 + NO2, HO2 H2O + NO2 and NO2 H2O + HO2, depending on the way the water interacts. Nitrogen Dioxide 124-127 heme oxygenase 2 Homo sapiens 118-121 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 43-46 heme oxygenase 2 Homo sapiens 37-40 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 43-46 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 43-46 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 188-191 heme oxygenase 2 Homo sapiens 37-40 25974050-1 2015 The kinetics of hydrogen abstraction by five radicals (H, O((3)P), OH, CH3, and HO2) from methyl acetate (MA) is investigated theoretically in order to gain further understanding of certain aspects of the combustion chemistry of biodiesels, such as the effect of the ester moiety. methyl acetate 90-104 heme oxygenase 2 Homo sapiens 80-83 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 188-191 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 188-191 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 194-197 heme oxygenase 2 Homo sapiens 37-40 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 194-197 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 194-197 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 194-197 heme oxygenase 2 Homo sapiens 37-40 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 194-197 heme oxygenase 2 Homo sapiens 182-185 25974050-7 2015 The reactions involving the OH radical are predicted to have the highest rates among the five abstracting radicals, while those initiated by HO2 are expected to be the lowest. oh radical 28-38 heme oxygenase 2 Homo sapiens 141-144 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Nitrogen Dioxide 194-197 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 188-191 heme oxygenase 2 Homo sapiens 37-40 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 188-191 heme oxygenase 2 Homo sapiens 182-185 25988324-7 2015 The total rate constant of the H2O HO2 + NO2 reaction is estimated to be slower than the naked reaction by 6 orders of magnitude at 298 K. However, the total rate constants of the HO2 H2O + NO2 and NO2 H2O + HO2 reactions are faster than the naked reaction by 4 and 3 orders of magnitude at 298 K, respectively. Water 188-191 heme oxygenase 2 Homo sapiens 182-185 25486386-3 2015 The alpha-diketone likely results from HOx-neutral chemistry previously only known to occur in reactions of HO2 with halogenated peroxy radicals. alpha-diketone 4-18 heme oxygenase 2 Homo sapiens 108-111 25486386-3 2015 The alpha-diketone likely results from HOx-neutral chemistry previously only known to occur in reactions of HO2 with halogenated peroxy radicals. hydrogen oxalate 39-42 heme oxygenase 2 Homo sapiens 108-111 25486386-0 2015 Atmospheric fate of methyl vinyl ketone: peroxy radical reactions with NO and HO2. 3-buten-2-one 20-39 heme oxygenase 2 Homo sapiens 78-81 25486386-3 2015 The alpha-diketone likely results from HOx-neutral chemistry previously only known to occur in reactions of HO2 with halogenated peroxy radicals. peroxy radicals 129-144 heme oxygenase 2 Homo sapiens 108-111 25849895-2 2015 Mammals contain two isoforms of this enzyme, HO2 and HO1, which share the same alpha-helical fold forming the catalytic core and heme binding site, as well as a membrane spanning helix at their C-termini. Heme 129-133 heme oxygenase 2 Homo sapiens 45-48 25849895-3 2015 However, unlike HO1, HO2 has an additional 30-residue N-terminus as well as two cysteine-proline sequences near the C-terminus that reside in heme regulatory motifs (HRMs). Cysteine 80-88 heme oxygenase 2 Homo sapiens 21-24 25853617-2 2015 Previous studies using the soluble form of human HO2 spanning residues 1-288 (HO2sol) have shown that a disulfide bond forms between Cys265 and Cys282 and that, in this oxidized state, heme binds to the catalytic site of HO2sol via His45. Heme 185-189 heme oxygenase 2 Homo sapiens 78-81 25853617-4 2015 In an effort to understand how the HRMs are involved in binding of heme to disulfide-reduced HO2sol, in the work described here, we further investigated the properties of Fe(3+)-heme bound to HO2. Heme 67-71 heme oxygenase 2 Homo sapiens 93-96 25849895-3 2015 However, unlike HO1, HO2 has an additional 30-residue N-terminus as well as two cysteine-proline sequences near the C-terminus that reside in heme regulatory motifs (HRMs). Heme 142-146 heme oxygenase 2 Homo sapiens 21-24 25853617-4 2015 In an effort to understand how the HRMs are involved in binding of heme to disulfide-reduced HO2sol, in the work described here, we further investigated the properties of Fe(3+)-heme bound to HO2. Disulfides 75-84 heme oxygenase 2 Homo sapiens 93-96 25849895-4 2015 While the role of the additional N-terminal residues of HO2 is not yet understood, the HRMs have been proposed to reversibly form a thiol/disulfide redox switch that modulates the affinity of HO2 for ferric heme as a function of cellular redox poise. Sulfhydryl Compounds 132-137 heme oxygenase 2 Homo sapiens 192-195 25849895-4 2015 While the role of the additional N-terminal residues of HO2 is not yet understood, the HRMs have been proposed to reversibly form a thiol/disulfide redox switch that modulates the affinity of HO2 for ferric heme as a function of cellular redox poise. Disulfides 138-147 heme oxygenase 2 Homo sapiens 192-195 25853617-5 2015 Specifically, we investigated binding of Fe(3+)-heme to a truncated form of soluble HO2 (residues 213-288; HO2tail) that spans the C-terminal HRMs of HO2 but lacks the catalytic core. fe(3+)-heme 41-52 heme oxygenase 2 Homo sapiens 84-87 25849895-4 2015 While the role of the additional N-terminal residues of HO2 is not yet understood, the HRMs have been proposed to reversibly form a thiol/disulfide redox switch that modulates the affinity of HO2 for ferric heme as a function of cellular redox poise. ferric heme 200-211 heme oxygenase 2 Homo sapiens 192-195 25853617-5 2015 Specifically, we investigated binding of Fe(3+)-heme to a truncated form of soluble HO2 (residues 213-288; HO2tail) that spans the C-terminal HRMs of HO2 but lacks the catalytic core. fe(3+)-heme 41-52 heme oxygenase 2 Homo sapiens 107-110 25853617-5 2015 Specifically, we investigated binding of Fe(3+)-heme to a truncated form of soluble HO2 (residues 213-288; HO2tail) that spans the C-terminal HRMs of HO2 but lacks the catalytic core. ho2tail 107-114 heme oxygenase 2 Homo sapiens 84-87 25853617-6 2015 We found that HO2tail in the disulfide-reduced state binds Fe(3+)-heme and accounts for the spectral features observed upon binding of heme to the disulfide-reduced form of HO2sol that cannot be attributed to heme binding at the catalytic site. Disulfides 29-38 heme oxygenase 2 Homo sapiens 14-17 25853617-6 2015 We found that HO2tail in the disulfide-reduced state binds Fe(3+)-heme and accounts for the spectral features observed upon binding of heme to the disulfide-reduced form of HO2sol that cannot be attributed to heme binding at the catalytic site. fe(3+)-heme 59-70 heme oxygenase 2 Homo sapiens 14-17 25853617-6 2015 We found that HO2tail in the disulfide-reduced state binds Fe(3+)-heme and accounts for the spectral features observed upon binding of heme to the disulfide-reduced form of HO2sol that cannot be attributed to heme binding at the catalytic site. Heme 66-70 heme oxygenase 2 Homo sapiens 14-17 25853617-6 2015 We found that HO2tail in the disulfide-reduced state binds Fe(3+)-heme and accounts for the spectral features observed upon binding of heme to the disulfide-reduced form of HO2sol that cannot be attributed to heme binding at the catalytic site. Disulfides 147-156 heme oxygenase 2 Homo sapiens 14-17 25853617-6 2015 We found that HO2tail in the disulfide-reduced state binds Fe(3+)-heme and accounts for the spectral features observed upon binding of heme to the disulfide-reduced form of HO2sol that cannot be attributed to heme binding at the catalytic site. Heme 135-139 heme oxygenase 2 Homo sapiens 14-17 25853617-10 2015 In summary, disulfide-reduced HO2 has multiple binding sites with varying affinities for Fe(3+)-heme. Disulfides 12-21 heme oxygenase 2 Homo sapiens 30-33 25853617-10 2015 In summary, disulfide-reduced HO2 has multiple binding sites with varying affinities for Fe(3+)-heme. fe(3+)-heme 89-100 heme oxygenase 2 Homo sapiens 30-33 25849895-7 2015 However, protein NMR experiments illustrate that, under reducing conditions, the C-terminal region gains some structure as the Cys residues in the HRMs undergo reduction (HO2(R)) and, in experiments employing a diamagnetic protoporphyrin, suggest a redox-dependent interaction between the core and the HRM domains. Cysteine 127-130 heme oxygenase 2 Homo sapiens 171-174 25849895-9 2015 Taken together with EPR measurements, which show the appearance of a new low-spin heme signal in reduced HO2, it appears that a cysteine residue(s) in the HRMs directly interacts with a second bound heme. Heme 82-86 heme oxygenase 2 Homo sapiens 105-108 25849895-9 2015 Taken together with EPR measurements, which show the appearance of a new low-spin heme signal in reduced HO2, it appears that a cysteine residue(s) in the HRMs directly interacts with a second bound heme. Cysteine 128-136 heme oxygenase 2 Homo sapiens 105-108 25849895-9 2015 Taken together with EPR measurements, which show the appearance of a new low-spin heme signal in reduced HO2, it appears that a cysteine residue(s) in the HRMs directly interacts with a second bound heme. Heme 199-203 heme oxygenase 2 Homo sapiens 105-108 25853617-0 2015 The C-terminal heme regulatory motifs of heme oxygenase-2 are redox-regulated heme binding sites. Heme 15-19 heme oxygenase 2 Homo sapiens 41-57 25853617-1 2015 Heme oxygenase-2 (HO2), an enzyme that catalyzes the conversion of heme to biliverdin, contains three heme regulatory motifs (HRMs) centered at Cys127, Cys265, and Cys282. Heme 67-71 heme oxygenase 2 Homo sapiens 0-16 25853617-1 2015 Heme oxygenase-2 (HO2), an enzyme that catalyzes the conversion of heme to biliverdin, contains three heme regulatory motifs (HRMs) centered at Cys127, Cys265, and Cys282. Heme 67-71 heme oxygenase 2 Homo sapiens 18-21 25853617-1 2015 Heme oxygenase-2 (HO2), an enzyme that catalyzes the conversion of heme to biliverdin, contains three heme regulatory motifs (HRMs) centered at Cys127, Cys265, and Cys282. Biliverdine 75-85 heme oxygenase 2 Homo sapiens 0-16 25853617-1 2015 Heme oxygenase-2 (HO2), an enzyme that catalyzes the conversion of heme to biliverdin, contains three heme regulatory motifs (HRMs) centered at Cys127, Cys265, and Cys282. Biliverdine 75-85 heme oxygenase 2 Homo sapiens 18-21 25853617-1 2015 Heme oxygenase-2 (HO2), an enzyme that catalyzes the conversion of heme to biliverdin, contains three heme regulatory motifs (HRMs) centered at Cys127, Cys265, and Cys282. Heme 102-106 heme oxygenase 2 Homo sapiens 0-16 25853617-1 2015 Heme oxygenase-2 (HO2), an enzyme that catalyzes the conversion of heme to biliverdin, contains three heme regulatory motifs (HRMs) centered at Cys127, Cys265, and Cys282. Heme 102-106 heme oxygenase 2 Homo sapiens 18-21 25853617-2 2015 Previous studies using the soluble form of human HO2 spanning residues 1-288 (HO2sol) have shown that a disulfide bond forms between Cys265 and Cys282 and that, in this oxidized state, heme binds to the catalytic site of HO2sol via His45. ho2sol 78-84 heme oxygenase 2 Homo sapiens 49-52 25853617-2 2015 Previous studies using the soluble form of human HO2 spanning residues 1-288 (HO2sol) have shown that a disulfide bond forms between Cys265 and Cys282 and that, in this oxidized state, heme binds to the catalytic site of HO2sol via His45. Disulfides 104-113 heme oxygenase 2 Homo sapiens 49-52 25853617-2 2015 Previous studies using the soluble form of human HO2 spanning residues 1-288 (HO2sol) have shown that a disulfide bond forms between Cys265 and Cys282 and that, in this oxidized state, heme binds to the catalytic site of HO2sol via His45. Disulfides 104-113 heme oxygenase 2 Homo sapiens 78-81 25853617-2 2015 Previous studies using the soluble form of human HO2 spanning residues 1-288 (HO2sol) have shown that a disulfide bond forms between Cys265 and Cys282 and that, in this oxidized state, heme binds to the catalytic site of HO2sol via His45. Heme 185-189 heme oxygenase 2 Homo sapiens 49-52 25811311-1 2015 Measurements of HO2 uptake coefficients (gamma) were made onto a variety of organic aerosols derived from glutaric acid, glyoxal, malonic acid, stearic acid, oleic acid, squalene, monoethanol amine sulfate, monomethyl amine sulfate, and two sources of humic acid, for an initial HO2 concentration of 1 x 10(9) molecules cm(-3), room temperature and at atmospheric pressure. glutaric acid 106-119 heme oxygenase 2 Homo sapiens 16-19 26633020-3 2015 The catechol moiety of Cat, Que, and rutin plays an essential role in concerted proton-coupled electron transfer (PCET) to HO2( ) derived from O2( -) to give H2O2 and the corresponding o-benzoquinone radical anions. catechol 4-12 heme oxygenase 2 Homo sapiens 123-126 25560388-10 2015 Since then, significant theoretical and experimental efforts have focused on determining the rate coefficients of primary n-butanol consumption pathways in combustion environments, including H atom abstraction reactions from n-butanol by key radicals such as HO2 and OH, as well as the decomposition of the radicals formed by these H atom abstractions. 1-Butanol 122-131 heme oxygenase 2 Homo sapiens 259-269 25556558-4 2015 HO2( )/( )O2(-) played the same important role as ( )OH in the AgBr-Ag-BiOBr photocatalytic system, and both the electron and hole were fully used for degradation of organic pollutants. Silver bromide 63-67 heme oxygenase 2 Homo sapiens 0-3 25556558-4 2015 HO2( )/( )O2(-) played the same important role as ( )OH in the AgBr-Ag-BiOBr photocatalytic system, and both the electron and hole were fully used for degradation of organic pollutants. bismuth oxybromide 71-76 heme oxygenase 2 Homo sapiens 0-3 25621533-1 2015 The absolute vacuum ultraviolet (VUV) photoionization spectra of the hydroperoxyl radical (HO2), hydrogen peroxide (H2O2), and formaldehyde (H2CO) have been measured from their first ionization thresholds to 12.008 eV. Hydroperoxy radical 69-89 heme oxygenase 2 Homo sapiens 91-94 25621533-2 2015 HO2, H2O2, and H2CO were generated from the oxidation of methanol initiated by pulsed-laser-photolysis of Cl2 in a low-pressure slow flow reactor. Methanol 57-65 heme oxygenase 2 Homo sapiens 0-3 25621533-2 2015 HO2, H2O2, and H2CO were generated from the oxidation of methanol initiated by pulsed-laser-photolysis of Cl2 in a low-pressure slow flow reactor. Chlorine 106-109 heme oxygenase 2 Homo sapiens 0-3 24456074-3 2015 To inactivate ROS cells biosynthesise several antioxidant enzymes, one of them is catalase which contributes H2 O2 to H2 O and O2 . Reactive Oxygen Species 14-17 heme oxygenase 2 Homo sapiens 109-129 26633020-3 2015 The catechol moiety of Cat, Que, and rutin plays an essential role in concerted proton-coupled electron transfer (PCET) to HO2( ) derived from O2( -) to give H2O2 and the corresponding o-benzoquinone radical anions. Quercetin 28-31 heme oxygenase 2 Homo sapiens 123-126 26633020-3 2015 The catechol moiety of Cat, Que, and rutin plays an essential role in concerted proton-coupled electron transfer (PCET) to HO2( ) derived from O2( -) to give H2O2 and the corresponding o-benzoquinone radical anions. Rutin 37-42 heme oxygenase 2 Homo sapiens 123-126 26633020-3 2015 The catechol moiety of Cat, Que, and rutin plays an essential role in concerted proton-coupled electron transfer (PCET) to HO2( ) derived from O2( -) to give H2O2 and the corresponding o-benzoquinone radical anions. pcet 114-118 heme oxygenase 2 Homo sapiens 123-126 26633020-3 2015 The catechol moiety of Cat, Que, and rutin plays an essential role in concerted proton-coupled electron transfer (PCET) to HO2( ) derived from O2( -) to give H2O2 and the corresponding o-benzoquinone radical anions. Hydrogen Peroxide 158-162 heme oxygenase 2 Homo sapiens 123-126 26633020-3 2015 The catechol moiety of Cat, Que, and rutin plays an essential role in concerted proton-coupled electron transfer (PCET) to HO2( ) derived from O2( -) to give H2O2 and the corresponding o-benzoquinone radical anions. o-benzoquinone radical 185-207 heme oxygenase 2 Homo sapiens 123-126 26633020-4 2015 On the other hand, the presence of alpha-TOH causes sequential electron and proton transfers to HO2( ) to give H2O2 and the alpha-tocopheroxyl radical. alpha-Tocopherol 35-44 heme oxygenase 2 Homo sapiens 96-99 26633020-4 2015 On the other hand, the presence of alpha-TOH causes sequential electron and proton transfers to HO2( ) to give H2O2 and the alpha-tocopheroxyl radical. Hydrogen Peroxide 111-115 heme oxygenase 2 Homo sapiens 96-99 26633020-4 2015 On the other hand, the presence of alpha-TOH causes sequential electron and proton transfers to HO2( ) to give H2O2 and the alpha-tocopheroxyl radical. alpha-Tocopheroxyl radical 124-150 heme oxygenase 2 Homo sapiens 96-99 25874340-0 2015 Novel imidazole derivatives as heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2) inhibitors and their cytotoxic activity in human-derived cancer cell lines. imidazole 6-15 heme oxygenase 2 Homo sapiens 77-81 25874340-2 2015 In this work, novel imidazole derivatives were designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2). imidazole 20-29 heme oxygenase 2 Homo sapiens 135-139 25127247-5 2015 Knowing that the H2O2 measured experimentally during sonication of water comes from the recombination of hydroxyl (OH) and perhydroxyl (HO2) radicals in the liquid phase and assuming that in sonochemistry applications, the cavitation is transient and the bubble fragments at the first collapse, the number of bubbles formed per unit time per unit volume is then easily determined using material balances for H2O2, OH and HO2 in the liquid phase. Hydrogen Peroxide 17-21 heme oxygenase 2 Homo sapiens 136-139 25127247-5 2015 Knowing that the H2O2 measured experimentally during sonication of water comes from the recombination of hydroxyl (OH) and perhydroxyl (HO2) radicals in the liquid phase and assuming that in sonochemistry applications, the cavitation is transient and the bubble fragments at the first collapse, the number of bubbles formed per unit time per unit volume is then easily determined using material balances for H2O2, OH and HO2 in the liquid phase. Hydrogen Peroxide 17-21 heme oxygenase 2 Homo sapiens 421-424 25127247-5 2015 Knowing that the H2O2 measured experimentally during sonication of water comes from the recombination of hydroxyl (OH) and perhydroxyl (HO2) radicals in the liquid phase and assuming that in sonochemistry applications, the cavitation is transient and the bubble fragments at the first collapse, the number of bubbles formed per unit time per unit volume is then easily determined using material balances for H2O2, OH and HO2 in the liquid phase. Water 67-72 heme oxygenase 2 Homo sapiens 136-139 25127247-5 2015 Knowing that the H2O2 measured experimentally during sonication of water comes from the recombination of hydroxyl (OH) and perhydroxyl (HO2) radicals in the liquid phase and assuming that in sonochemistry applications, the cavitation is transient and the bubble fragments at the first collapse, the number of bubbles formed per unit time per unit volume is then easily determined using material balances for H2O2, OH and HO2 in the liquid phase. Water 67-72 heme oxygenase 2 Homo sapiens 421-424 25127247-5 2015 Knowing that the H2O2 measured experimentally during sonication of water comes from the recombination of hydroxyl (OH) and perhydroxyl (HO2) radicals in the liquid phase and assuming that in sonochemistry applications, the cavitation is transient and the bubble fragments at the first collapse, the number of bubbles formed per unit time per unit volume is then easily determined using material balances for H2O2, OH and HO2 in the liquid phase. Hydrogen Peroxide 408-412 heme oxygenase 2 Homo sapiens 136-139 25381864-1 2014 For the first time quantitative measurements of the hydroperoxyl radical (HO2) in a jet-stirred reactor were performed thanks to a new experimental setup involving fast sampling and near-infrared cavity ring-down spectroscopy at low pressure. Hydroperoxy radical 52-72 heme oxygenase 2 Homo sapiens 74-77 25387985-0 2014 Theoretical chemical kinetic study of the H-atom abstraction reactions from aldehydes and acids by H atoms and OH, HO2, and CH3 radicals. Aldehydes 76-85 heme oxygenase 2 Homo sapiens 115-118 25387985-4 2014 For the reactions of methanal and methanoic acid with H atoms and OH, HO2, and CH3 radicals, the calculated relative electronic energies were obtained with the CCSD(T)/cc-pVXZ (where X = D, T, and Q) method and were extrapolated to the complete basis set limit. Formaldehyde 21-29 heme oxygenase 2 Homo sapiens 70-73 25387985-4 2014 For the reactions of methanal and methanoic acid with H atoms and OH, HO2, and CH3 radicals, the calculated relative electronic energies were obtained with the CCSD(T)/cc-pVXZ (where X = D, T, and Q) method and were extrapolated to the complete basis set limit. formic acid 34-48 heme oxygenase 2 Homo sapiens 70-73 25381864-5 2014 Measuring HO2 formation from hydrocarbon oxidation is extremely important in determining the propensity of a fuel to follow chain-termination pathways from R + O2 compared to chain branching (leading to OH), helping to constrain and better validate detailed chemical kinetics models. Hydrocarbons 29-40 heme oxygenase 2 Homo sapiens 10-13 24997963-4 2014 The CB-OH adducts react with O2 either by irreversible H-abstraction to form chlorophenol and HO2 or by reversible additions to form CB-OH-O2 radicals, which subsequently cyclize to bicyclic radicals. cb-oh 4-9 heme oxygenase 2 Homo sapiens 94-97 25320837-3 2014 In the atmosphere, R2 and R4 react with O2 by irreversible H-abstraction to dimethylphenols or by reversible additions to bicyclic radical intermediates, which would recombine again with O2 to form bicyclic peroxy radicals, to bicyclic alkoxyl radicals by reacting with NO or HO2, and eventually to final products such as glyoxal, methylglyoxal, and their coproducts. Oxygen 40-42 heme oxygenase 2 Homo sapiens 276-279 24965004-3 2014 During radiolysis of aerated solutions hydroxyl radical (( )OH), eaq (-), H( ) and O2 ( -)/HO2 ( ) reactive intermediates are produced, the degradation of solute takes place practically entirely through ( )OH reactions. Oxygen 83-85 heme oxygenase 2 Homo sapiens 91-94 24965004-8 2014 The latter may eliminate HO2 ( ) giving phenols or undergoes fragmentation. Phenols 40-47 heme oxygenase 2 Homo sapiens 25-28 25196843-5 2014 The (1)H-(15)N TROSY NMR spectrum of HO-2 reveals specific residues, including Leu-201, near the heme face of HO-2 that are affected by the addition of CPR, implicating these residues at the HO/CPR interface. Leucine 79-82 heme oxygenase 2 Homo sapiens 37-41 25196843-5 2014 The (1)H-(15)N TROSY NMR spectrum of HO-2 reveals specific residues, including Leu-201, near the heme face of HO-2 that are affected by the addition of CPR, implicating these residues at the HO/CPR interface. Leucine 79-82 heme oxygenase 2 Homo sapiens 110-114 25196843-5 2014 The (1)H-(15)N TROSY NMR spectrum of HO-2 reveals specific residues, including Leu-201, near the heme face of HO-2 that are affected by the addition of CPR, implicating these residues at the HO/CPR interface. Heme 97-101 heme oxygenase 2 Homo sapiens 37-41 25196843-5 2014 The (1)H-(15)N TROSY NMR spectrum of HO-2 reveals specific residues, including Leu-201, near the heme face of HO-2 that are affected by the addition of CPR, implicating these residues at the HO/CPR interface. Heme 97-101 heme oxygenase 2 Homo sapiens 110-114 25196843-6 2014 Alanine substitutions at HO-2 residues Leu-201 and Lys-169 cause a respective 3- and 22-fold increase in K(m) values for CPR, consistent with a role for these residues in CPR binding. Alanine 0-7 heme oxygenase 2 Homo sapiens 25-29 25196843-6 2014 Alanine substitutions at HO-2 residues Leu-201 and Lys-169 cause a respective 3- and 22-fold increase in K(m) values for CPR, consistent with a role for these residues in CPR binding. Leucine 39-42 heme oxygenase 2 Homo sapiens 25-29 25196843-6 2014 Alanine substitutions at HO-2 residues Leu-201 and Lys-169 cause a respective 3- and 22-fold increase in K(m) values for CPR, consistent with a role for these residues in CPR binding. Lysine 51-54 heme oxygenase 2 Homo sapiens 25-29 24997963-4 2014 The CB-OH adducts react with O2 either by irreversible H-abstraction to form chlorophenol and HO2 or by reversible additions to form CB-OH-O2 radicals, which subsequently cyclize to bicyclic radicals. Oxygen 29-31 heme oxygenase 2 Homo sapiens 94-97 24997964-0 2014 The atmospheric degradation pathways of BrCH2O2: computational calculation on mechanisms of the reaction with HO2. brch2o2 40-47 heme oxygenase 2 Homo sapiens 110-113 24997964-1 2014 Mechanisms for the atmospheric degradation reaction of BrCH2O2+HO2 were investigated using quantum chemistry methods. brch2o2 55-62 heme oxygenase 2 Homo sapiens 63-66 24997964-3 2014 While CH2O+HBr+O3, BrCHO+OH+HO2 and CH2O+Br+HO3 will be competitive to a certain extent in the atmosphere. brcho 19-24 heme oxygenase 2 Homo sapiens 28-31 24997964-7 2014 Comparisons indicate that halogen substitution effect makes minor contributions to the XCH2O2 (X=H, F, Cl and Br)+HO2 reactions in the atmosphere. Halogens 26-33 heme oxygenase 2 Homo sapiens 114-117 24997964-7 2014 Comparisons indicate that halogen substitution effect makes minor contributions to the XCH2O2 (X=H, F, Cl and Br)+HO2 reactions in the atmosphere. xch2o2 87-93 heme oxygenase 2 Homo sapiens 114-117 24997964-7 2014 Comparisons indicate that halogen substitution effect makes minor contributions to the XCH2O2 (X=H, F, Cl and Br)+HO2 reactions in the atmosphere. Fluorine 100-101 heme oxygenase 2 Homo sapiens 114-117 24997964-7 2014 Comparisons indicate that halogen substitution effect makes minor contributions to the XCH2O2 (X=H, F, Cl and Br)+HO2 reactions in the atmosphere. Bromine 110-112 heme oxygenase 2 Homo sapiens 114-117 24731472-1 2014 Application of Advanced Oxidation Processes (AOP) such as sono, photo and sonophoto catalysis in the purification of polluted water under ambient conditions involve the formation and participation of Reactive Oxygen Species (ROS) like OH, HO2 , O2(-), H2O2 etc. Water 126-131 heme oxygenase 2 Homo sapiens 240-243 25072999-2 2014 Titration of the carbon-centered radical, formed following the initial OH abstraction, with oxygen to give HO2 and an imine, followed by conversion of HO2 to OH by reaction with NO, resulted in biexponential OH decay traces on a millisecond time scale. Carbon 17-23 heme oxygenase 2 Homo sapiens 107-110 24731472-1 2014 Application of Advanced Oxidation Processes (AOP) such as sono, photo and sonophoto catalysis in the purification of polluted water under ambient conditions involve the formation and participation of Reactive Oxygen Species (ROS) like OH, HO2 , O2(-), H2O2 etc. Reactive Oxygen Species 200-223 heme oxygenase 2 Homo sapiens 240-243 24731472-1 2014 Application of Advanced Oxidation Processes (AOP) such as sono, photo and sonophoto catalysis in the purification of polluted water under ambient conditions involve the formation and participation of Reactive Oxygen Species (ROS) like OH, HO2 , O2(-), H2O2 etc. Reactive Oxygen Species 225-228 heme oxygenase 2 Homo sapiens 240-243 25072999-2 2014 Titration of the carbon-centered radical, formed following the initial OH abstraction, with oxygen to give HO2 and an imine, followed by conversion of HO2 to OH by reaction with NO, resulted in biexponential OH decay traces on a millisecond time scale. Carbon 17-23 heme oxygenase 2 Homo sapiens 151-154 25072999-2 2014 Titration of the carbon-centered radical, formed following the initial OH abstraction, with oxygen to give HO2 and an imine, followed by conversion of HO2 to OH by reaction with NO, resulted in biexponential OH decay traces on a millisecond time scale. radical 33-40 heme oxygenase 2 Homo sapiens 107-110 25072999-2 2014 Titration of the carbon-centered radical, formed following the initial OH abstraction, with oxygen to give HO2 and an imine, followed by conversion of HO2 to OH by reaction with NO, resulted in biexponential OH decay traces on a millisecond time scale. radical 33-40 heme oxygenase 2 Homo sapiens 151-154 25072999-2 2014 Titration of the carbon-centered radical, formed following the initial OH abstraction, with oxygen to give HO2 and an imine, followed by conversion of HO2 to OH by reaction with NO, resulted in biexponential OH decay traces on a millisecond time scale. Oxygen 92-98 heme oxygenase 2 Homo sapiens 107-110 25072999-2 2014 Titration of the carbon-centered radical, formed following the initial OH abstraction, with oxygen to give HO2 and an imine, followed by conversion of HO2 to OH by reaction with NO, resulted in biexponential OH decay traces on a millisecond time scale. Oxygen 92-98 heme oxygenase 2 Homo sapiens 151-154 25072999-2 2014 Titration of the carbon-centered radical, formed following the initial OH abstraction, with oxygen to give HO2 and an imine, followed by conversion of HO2 to OH by reaction with NO, resulted in biexponential OH decay traces on a millisecond time scale. Imines 118-123 heme oxygenase 2 Homo sapiens 151-154 24908009-2 2014 HCO radical and H atom yields have been quantified by time resolved continuous wave Cavity Ring Down Spectroscopy in the near infrared following their conversion to HO2 radicals by reaction with O2. hco radical 0-11 heme oxygenase 2 Homo sapiens 165-168 24894154-13 2014 The major reaction paths at 1000 K are formation of isooctane plus HO2 followed by cyclic ether plus OH. 2,2,4-trimethylpentane 52-61 heme oxygenase 2 Homo sapiens 67-70 24894154-13 2014 The major reaction paths at 1000 K are formation of isooctane plus HO2 followed by cyclic ether plus OH. Ethers, Cyclic 83-95 heme oxygenase 2 Homo sapiens 67-70 24908009-5 2014 Time resolved HO2 profiles under very low O2 concentrations suggest that another unknown HO2 forming reaction path exists in this reaction system besides the conversion of HCO radicals and H atoms by reaction with O2. Oxygen 15-17 heme oxygenase 2 Homo sapiens 89-92 24908009-5 2014 Time resolved HO2 profiles under very low O2 concentrations suggest that another unknown HO2 forming reaction path exists in this reaction system besides the conversion of HCO radicals and H atoms by reaction with O2. hco radicals 172-184 heme oxygenase 2 Homo sapiens 14-17 24908009-5 2014 Time resolved HO2 profiles under very low O2 concentrations suggest that another unknown HO2 forming reaction path exists in this reaction system besides the conversion of HCO radicals and H atoms by reaction with O2. hco radicals 172-184 heme oxygenase 2 Homo sapiens 89-92 24908009-5 2014 Time resolved HO2 profiles under very low O2 concentrations suggest that another unknown HO2 forming reaction path exists in this reaction system besides the conversion of HCO radicals and H atoms by reaction with O2. Oxygen 42-44 heme oxygenase 2 Homo sapiens 14-17 24908009-5 2014 Time resolved HO2 profiles under very low O2 concentrations suggest that another unknown HO2 forming reaction path exists in this reaction system besides the conversion of HCO radicals and H atoms by reaction with O2. Oxygen 42-44 heme oxygenase 2 Homo sapiens 89-92 24908009-7 2014 The CH3O2 quantum yield has been determined in separate experiments as phi(CH3) = 0.33 +- 0.03 and is in excellent agreement with the CH3 yields derived from the HO2 measurements considering that the triple fragmentation (R1e) is an important reaction path in the 248 nm photolysis of CH3CHO. Methyldioxy radical 4-9 heme oxygenase 2 Homo sapiens 162-165 24798952-1 2014 Peroxy (HO2 and RO2) radicals are important intermediates in tropospheric oxidation of hydrocarbons, and their accurate atmospheric measurements remain challenging. Hydrocarbons 87-99 heme oxygenase 2 Homo sapiens 8-11 24359921-4 2014 Photolysis of the Fe(III)-oxalato complex was favorable due to the formation of O2-, HO2 and OH for oxidizing the dye; however, an excess of H2O2 could quench the excited state of ferrioxalate, decreasing the degradation efficiency. fe(iii)-oxalato 18-33 heme oxygenase 2 Homo sapiens 85-88 24644296-11 2014 The adsorption of NH3 as a probe molecule indicates that the acidity can affect the hydrogen-bonding interaction between (N-H O2) and (N H-O2). Ammonia 18-21 heme oxygenase 2 Homo sapiens 141-145 24644296-11 2014 The adsorption of NH3 as a probe molecule indicates that the acidity can affect the hydrogen-bonding interaction between (N-H O2) and (N H-O2). Hydrogen 84-92 heme oxygenase 2 Homo sapiens 141-145 24644296-11 2014 The adsorption of NH3 as a probe molecule indicates that the acidity can affect the hydrogen-bonding interaction between (N-H O2) and (N H-O2). Oxygen 128-130 heme oxygenase 2 Homo sapiens 141-145 24862399-13 2014 CONCLUSION: Alteration of serum triglycerides and HDL-C significantly impairs HO-1 and HO-2 levels in benign prostatic hyperplasia patients. Triglycerides 32-45 heme oxygenase 2 Homo sapiens 87-91 24745305-1 2014 Relative rate studies were carried out to determine the temperature dependent rate constant ratio k1/k2a: CH3O + O2 HCHO + HO2 and CH3O + NO2 (+M) CH3ONO2 (+M) over the temperature range 250-333 K in an environmental chamber at 700 Torr using Fourier transform infrared detection. 7-methoxy-6-(2'-methoxy-3'-hydroxy-3'-methyl butyl) 106-110 heme oxygenase 2 Homo sapiens 126-129 24180608-1 2014 SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin. Heme 112-116 heme oxygenase 2 Homo sapiens 67-71 24754561-2 2014 In this system, H( ) (or HO2( ) in the presence of dissolved oxygen) and H2O2 produced by the radiolytic decomposition of water both reduce Ce(4+) ions to Ce(3+) ions, while ( )OH radicals oxidize the Ce(3+) present in the solution back to Ce(4+). Oxygen 61-67 heme oxygenase 2 Homo sapiens 25-28 24754561-2 2014 In this system, H( ) (or HO2( ) in the presence of dissolved oxygen) and H2O2 produced by the radiolytic decomposition of water both reduce Ce(4+) ions to Ce(3+) ions, while ( )OH radicals oxidize the Ce(3+) present in the solution back to Ce(4+). Water 122-127 heme oxygenase 2 Homo sapiens 25-28 24754561-2 2014 In this system, H( ) (or HO2( ) in the presence of dissolved oxygen) and H2O2 produced by the radiolytic decomposition of water both reduce Ce(4+) ions to Ce(3+) ions, while ( )OH radicals oxidize the Ce(3+) present in the solution back to Ce(4+). ( )oh radicals 174-188 heme oxygenase 2 Homo sapiens 25-28 24180608-1 2014 SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin. Carbon Monoxide 120-135 heme oxygenase 2 Homo sapiens 67-71 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Heme 90-94 heme oxygenase 2 Homo sapiens 40-44 24180608-1 2014 SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin. Carbon Monoxide 137-139 heme oxygenase 2 Homo sapiens 67-71 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Carbon Monoxide 100-115 heme oxygenase 2 Homo sapiens 40-44 24180608-1 2014 SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin. Biliverdine 162-172 heme oxygenase 2 Homo sapiens 67-71 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Carbon Monoxide 117-119 heme oxygenase 2 Homo sapiens 40-44 23641685-1 2013 We report vibrational and electronic spectra of the hydroxy-methyl-peroxy radical (HOCH2OO( ) or HMP), which was formed as the primary product of the reaction of the hydroperoxy radical, HO2( ), and formaldehyde, HCHO. hydroxy-methyl-peroxy radical 52-81 heme oxygenase 2 Homo sapiens 187-190 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Iron 122-126 heme oxygenase 2 Homo sapiens 40-44 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Biliverdine 132-142 heme oxygenase 2 Homo sapiens 40-44 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Bilirubin 179-188 heme oxygenase 2 Homo sapiens 40-44 24483837-0 2014 Rate constant calculations of H-atom abstraction reactions from ethers by HO2 radicals. Ethers 64-70 heme oxygenase 2 Homo sapiens 74-77 24483837-5 2014 As a benchmark in the electronic energy calculations, the CCSD(T)/CBS extrapolation was used for the reactions of dimethyl ether + HO2 radicals. dimethyl ether 114-128 heme oxygenase 2 Homo sapiens 131-134 24533775-1 2014 BACKGROUND: Previously, we reported that menadione activated rat, native heme oxygenase-2 (HO-2) and human recombinant heme oxygenase-2 selectively; it did not activate spleen, microsomal heme oxygenase-1. Vitamin K 3 41-50 heme oxygenase 2 Homo sapiens 119-135 24533775-8 2014 Menadione activated full-length recombinant human heme oxygenase-2 (FL-hHO-2) as effectively as rat brain enzyme, but it did not activate rat spleen heme oxygenase. Vitamin K 3 0-9 heme oxygenase 2 Homo sapiens 50-66 24400665-5 2014 An enhanced importance of the reactions via the Waddington mechanism and of those of allylic radicals with HO2 radicals can be noted for 2- and 3-hexenes compared to 1-hexene. 2- and 3-hexenes 137-153 heme oxygenase 2 Homo sapiens 107-110 24400665-5 2014 An enhanced importance of the reactions via the Waddington mechanism and of those of allylic radicals with HO2 radicals can be noted for 2- and 3-hexenes compared to 1-hexene. 1-hexene 166-174 heme oxygenase 2 Homo sapiens 107-110 25302388-5 2014 We will particularly focus on the formation of two OH radicals by the reaction H + HO2. two oh radicals 47-62 heme oxygenase 2 Homo sapiens 83-86 25136403-11 2014 Finally, we call attention on the role of HO-2 in oxygen sensing, discussing proposed hypothesis on heme binding motifs and redox/thiol switches that participate in oxygen sensing as well as evidences of HO-2 response to hypoxia. Oxygen 50-56 heme oxygenase 2 Homo sapiens 42-46 24277836-0 2013 Quantification of OH and HO2 radicals during the low-temperature oxidation of hydrocarbons by Fluorescence Assay by Gas Expansion technique. Hydrocarbons 78-90 heme oxygenase 2 Homo sapiens 25-28 24171583-2 2013 Alkene ozonolysis is also known to directly form HO2 radicals, which may be readily converted to OH through reaction with NO, but whose formation is poorly understood. Alkenes 0-6 heme oxygenase 2 Homo sapiens 49-52 24171583-3 2013 We report a study of the radical (OH, HO2, and RO2) production from a series of small alkenes (propene, 1-butene, cis-2-butene, trans-2-butene, 2-methylpropene, 2,3-dimethyl-2-butene (tetramethyl ethene, TME), and isoprene). radical 25-32 heme oxygenase 2 Homo sapiens 38-41 24171583-3 2013 We report a study of the radical (OH, HO2, and RO2) production from a series of small alkenes (propene, 1-butene, cis-2-butene, trans-2-butene, 2-methylpropene, 2,3-dimethyl-2-butene (tetramethyl ethene, TME), and isoprene). Alkenes 86-93 heme oxygenase 2 Homo sapiens 38-41 24171583-6 2013 HO2 yields ranged from 4% (trans-2-butene) to 34% (2-methylpropene), lower than previous experimental determinations. 2-butene 27-41 heme oxygenase 2 Homo sapiens 0-3 24171583-6 2013 HO2 yields ranged from 4% (trans-2-butene) to 34% (2-methylpropene), lower than previous experimental determinations. isobutylene 51-66 heme oxygenase 2 Homo sapiens 0-3 24171583-7 2013 Increasing humidity further reduced the HO2 yields obtained, by typically 50% for an RH increase from 0.5 to 30%, suggesting that HOx production from alkene ozonolysis may be lower than current models suggest under (humid) ambient atmospheric boundary layer conditions. hydrogen oxalate 130-133 heme oxygenase 2 Homo sapiens 40-43 24171583-7 2013 Increasing humidity further reduced the HO2 yields obtained, by typically 50% for an RH increase from 0.5 to 30%, suggesting that HOx production from alkene ozonolysis may be lower than current models suggest under (humid) ambient atmospheric boundary layer conditions. Alkenes 150-156 heme oxygenase 2 Homo sapiens 40-43 24021581-0 2013 Selective inhibition of heme oxygenase-2 activity by analogs of 1-(4-chlorobenzyl)-2-(pyrrolidin-1-ylmethyl)-1H-benzimidazole (clemizole): Exploration of the effects of substituents at the N-1 position. clemizole 64-125 heme oxygenase 2 Homo sapiens 24-40 24021581-0 2013 Selective inhibition of heme oxygenase-2 activity by analogs of 1-(4-chlorobenzyl)-2-(pyrrolidin-1-ylmethyl)-1H-benzimidazole (clemizole): Exploration of the effects of substituents at the N-1 position. clemizole 127-136 heme oxygenase 2 Homo sapiens 24-40 24273333-11 2013 The chemically activated recombination of HO2 or CH3O2 with the 5-methyl-2-furanylmethyl radical, forming a 5-methyl-2-furylmethanoxy radical and OH or CH3O radical is also found to exhibit significant control over ignition delay times, as well as being important reactions in the prediction of species profiles in a JSR. Methyldioxy radical 49-54 heme oxygenase 2 Homo sapiens 42-45 24273333-11 2013 The chemically activated recombination of HO2 or CH3O2 with the 5-methyl-2-furanylmethyl radical, forming a 5-methyl-2-furylmethanoxy radical and OH or CH3O radical is also found to exhibit significant control over ignition delay times, as well as being important reactions in the prediction of species profiles in a JSR. 5-methyl-2-furanylmethyl radical 64-96 heme oxygenase 2 Homo sapiens 42-45 24273333-11 2013 The chemically activated recombination of HO2 or CH3O2 with the 5-methyl-2-furanylmethyl radical, forming a 5-methyl-2-furylmethanoxy radical and OH or CH3O radical is also found to exhibit significant control over ignition delay times, as well as being important reactions in the prediction of species profiles in a JSR. 5-methyl-2-furylmethanoxy radical 108-141 heme oxygenase 2 Homo sapiens 42-45 24273333-11 2013 The chemically activated recombination of HO2 or CH3O2 with the 5-methyl-2-furanylmethyl radical, forming a 5-methyl-2-furylmethanoxy radical and OH or CH3O radical is also found to exhibit significant control over ignition delay times, as well as being important reactions in the prediction of species profiles in a JSR. ch3o radical 152-164 heme oxygenase 2 Homo sapiens 42-45 24050618-10 2013 However, QuCN( ) can reduce O2 to O2( -), and this is followed by the protonation of O2( -) to afford HO2( ). qucn 9-13 heme oxygenase 2 Homo sapiens 102-105 24050618-11 2013 The hydrogen abstraction of HO2( ) from the F-adduct radical affords fluorobenzene and H2O2 as the final products. Hydrogen 4-12 heme oxygenase 2 Homo sapiens 28-31 24050618-11 2013 The hydrogen abstraction of HO2( ) from the F-adduct radical affords fluorobenzene and H2O2 as the final products. Fluorobenzenes 69-82 heme oxygenase 2 Homo sapiens 28-31 24050618-11 2013 The hydrogen abstraction of HO2( ) from the F-adduct radical affords fluorobenzene and H2O2 as the final products. Hydrogen Peroxide 87-91 heme oxygenase 2 Homo sapiens 28-31 24095673-9 2014 Strikingly, HO2 radicals were an order of magnitude more concentrated in the headgroups region than in water, implying a large shift in the acid-base equilibrium between HO2 and O2(-). Water 103-108 heme oxygenase 2 Homo sapiens 12-15 24095673-9 2014 Strikingly, HO2 radicals were an order of magnitude more concentrated in the headgroups region than in water, implying a large shift in the acid-base equilibrium between HO2 and O2(-). Oxygen 13-15 heme oxygenase 2 Homo sapiens 170-173 24275768-1 2014 PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide. Heme 70-74 heme oxygenase 2 Homo sapiens 122-126 24275768-1 2014 PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide. Biliverdine 165-175 heme oxygenase 2 Homo sapiens 122-126 24275768-1 2014 PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide. Iron 187-191 heme oxygenase 2 Homo sapiens 122-126 24275768-1 2014 PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide. Carbon Monoxide 207-222 heme oxygenase 2 Homo sapiens 122-126 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. Hydrogen 65-73 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. Hydroperoxy radical 108-128 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. Esters 152-158 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. methyl acetate 160-176 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. METHYL PROPIONATE 178-195 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. methyl butyrate 197-213 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. METHYL VALERATE 215-232 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. METHYL ISOBUTYRATE 234-252 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. ethyl acetate 161-176 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. propyl acetate 271-287 heme oxygenase 2 Homo sapiens 130-133 24175616-2 2013 This work details an ab initio and chemical kinetic study of the hydrogen atom abstraction reactions by the hydroperoxyl radical (HO2) on the following esters: methyl ethanoate, methyl propanoate, methyl butanoate, methyl pentanoate, methyl isobutyrate, ethyl ethanoate, propyl ethanoate, and isopropyl ethanoate. isopropyl acetate 293-312 heme oxygenase 2 Homo sapiens 130-133 24175616-6 2013 The CCSD(T)/CBS (extrapolated from CCSD(T)/cc-pVXZ, in which X = D, T, Q) was used for the reactions of methyl ethanoate + HO2 radicals as a benchmark in the electronic energy calculations. methyl acetate 104-120 heme oxygenase 2 Homo sapiens 123-126 23808372-5 2013 The 1-hydroxybut-1-yl + O2 reaction is dominated by direct HO2 elimination from the corresponding peroxy radical forming butanal as the stable coproduct. 1-hydroxybut-1-yl + o2 4-26 heme oxygenase 2 Homo sapiens 59-62 23808372-5 2013 The 1-hydroxybut-1-yl + O2 reaction is dominated by direct HO2 elimination from the corresponding peroxy radical forming butanal as the stable coproduct. Oxygen 98-112 heme oxygenase 2 Homo sapiens 59-62 23992228-3 2013 RESULTS: Carbon monoxide derived from haem oxygenase (HO)-2 is predominantly involved in neuromodulation and in setting the smooth muscle membrane potential, while CO derived from HO-1 has anti-inflammatory and antioxidative properties, which protect gastrointestinal smooth muscle from damage caused by injury or inflammation. Carbon Monoxide 9-24 heme oxygenase 2 Homo sapiens 38-59 23641685-1 2013 We report vibrational and electronic spectra of the hydroxy-methyl-peroxy radical (HOCH2OO( ) or HMP), which was formed as the primary product of the reaction of the hydroperoxy radical, HO2( ), and formaldehyde, HCHO. HOCH2O2 83-90 heme oxygenase 2 Homo sapiens 187-190 23641685-1 2013 We report vibrational and electronic spectra of the hydroxy-methyl-peroxy radical (HOCH2OO( ) or HMP), which was formed as the primary product of the reaction of the hydroperoxy radical, HO2( ), and formaldehyde, HCHO. perhydroxyl radical 166-185 heme oxygenase 2 Homo sapiens 187-190 23641685-1 2013 We report vibrational and electronic spectra of the hydroxy-methyl-peroxy radical (HOCH2OO( ) or HMP), which was formed as the primary product of the reaction of the hydroperoxy radical, HO2( ), and formaldehyde, HCHO. Formaldehyde 199-211 heme oxygenase 2 Homo sapiens 187-190 23867846-6 2013 For example, the HO2/OH ratios from the CMAQ model simulations with GEIA isoprene emissions were 2.7 times larger than those from the CMAQ model simulations based on MEGAN isoprene emissions. geia isoprene 68-81 heme oxygenase 2 Homo sapiens 17-20 23867846-6 2013 For example, the HO2/OH ratios from the CMAQ model simulations with GEIA isoprene emissions were 2.7 times larger than those from the CMAQ model simulations based on MEGAN isoprene emissions. megan isoprene 166-180 heme oxygenase 2 Homo sapiens 17-20 23867846-7 2013 The large HO2/OH ratios from the CMAQ model simulations with the GEIA biogenic emission were possibly due to the overestimation of GEIA biogenic isoprene emissions over East Asia. isoprene 145-153 heme oxygenase 2 Homo sapiens 10-13 23960019-1 2013 An intramolecular bifurcated H-bond from the axial HO-2 group to the axial F-4 atom and to the O5 atom of alpha-D-hexopyranosides in apolar solvents is evidenced in (1)H NMR spectra. alpha-d-hexopyranosides 106-129 heme oxygenase 2 Homo sapiens 51-55 26283246-2 2013 It is demonstrated that the effect of quantum tunneling corrections for the reaction HO2 + HO2 = H2O2 + O2 can have a noticeable impact on the performance of a high-fidelity model of a compression-ignition (e.g., diesel) engine, and that an accurate prediction of ignition delay time for the engine model requires an accurate estimation of the tunneling correction for this reaction. Hydrogen Peroxide 97-101 heme oxygenase 2 Homo sapiens 85-88 23770489-2 2013 The results showed that the natural montmorillonite induced the photooxidation of As(III) by generating hydroxyl radicals (HO ) and hydroperoxyl/superoxide radicals (HO2 /O2- ). Bentonite 36-51 heme oxygenase 2 Homo sapiens 166-169 23770489-2 2013 The results showed that the natural montmorillonite induced the photooxidation of As(III) by generating hydroxyl radicals (HO ) and hydroperoxyl/superoxide radicals (HO2 /O2- ). as(iii) 82-89 heme oxygenase 2 Homo sapiens 166-169 23770489-2 2013 The results showed that the natural montmorillonite induced the photooxidation of As(III) by generating hydroxyl radicals (HO ) and hydroperoxyl/superoxide radicals (HO2 /O2- ). hydroperoxyl/superoxide radicals 132-164 heme oxygenase 2 Homo sapiens 166-169 23770489-4 2013 Approximately 38% of HO was generated by the photolysis of ferric ions, and the formation of the remaining 62% was strongly dependent on the HO2 /O2- . Hydroxyl Radical 21-23 heme oxygenase 2 Homo sapiens 142-145 23867390-1 2013 A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2). 1,2,4-triazole 60-74 heme oxygenase 2 Homo sapiens 157-173 23867390-1 2013 A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2). 1,2,4-triazole 60-74 heme oxygenase 2 Homo sapiens 175-179 23806979-0 2013 Measurements of uptake coefficients for heterogeneous loss of HO2 onto submicron inorganic salt aerosols. inorganic salt 81-95 heme oxygenase 2 Homo sapiens 62-65 23806979-1 2013 Laboratory studies were conducted to investigate the kinetics of HO2 radical uptake onto submicron inorganic salt aerosols. inorganic salt 99-113 heme oxygenase 2 Homo sapiens 65-68 23806979-3 2013 The uptake coefficient for HO2 uptake onto dry inorganic salt aerosols was consistently below the detection limit (gamma(HO2) < 0.004). inorganic salt 47-61 heme oxygenase 2 Homo sapiens 27-30 23806979-4 2013 The mass accommodation coefficient of HO2 radicals onto Cu(II)-doped (NH4)2SO4 aerosols was measured to be alpha(HO2) = 0.4 +- 0.3 representing the kinetic upper limit to gamma. cu(ii) 56-62 heme oxygenase 2 Homo sapiens 38-41 23806979-4 2013 The mass accommodation coefficient of HO2 radicals onto Cu(II)-doped (NH4)2SO4 aerosols was measured to be alpha(HO2) = 0.4 +- 0.3 representing the kinetic upper limit to gamma. cu(ii) 56-62 heme oxygenase 2 Homo sapiens 113-116 23806979-4 2013 The mass accommodation coefficient of HO2 radicals onto Cu(II)-doped (NH4)2SO4 aerosols was measured to be alpha(HO2) = 0.4 +- 0.3 representing the kinetic upper limit to gamma. Ammonium Sulfate 69-78 heme oxygenase 2 Homo sapiens 38-41 23806979-4 2013 The mass accommodation coefficient of HO2 radicals onto Cu(II)-doped (NH4)2SO4 aerosols was measured to be alpha(HO2) = 0.4 +- 0.3 representing the kinetic upper limit to gamma. Ammonium Sulfate 69-78 heme oxygenase 2 Homo sapiens 113-116 23806979-7 2013 Evidence is presented showing that the HO2 uptake coefficients onto aqueous salt aerosol particles are dependent both on the exposure time to the aerosol and on the HO2 concentration used. Salts 76-80 heme oxygenase 2 Homo sapiens 39-42 23806979-7 2013 Evidence is presented showing that the HO2 uptake coefficients onto aqueous salt aerosol particles are dependent both on the exposure time to the aerosol and on the HO2 concentration used. Salts 76-80 heme oxygenase 2 Homo sapiens 165-168 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). Alkenes 98-105 heme oxygenase 2 Homo sapiens 91-94 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). Alkenes 98-105 heme oxygenase 2 Homo sapiens 178-181 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). Alkenes 98-105 heme oxygenase 2 Homo sapiens 178-181 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). alkyl peroxy radical 156-176 heme oxygenase 2 Homo sapiens 91-94 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). alkyl peroxy radical 156-176 heme oxygenase 2 Homo sapiens 178-181 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). alkyl peroxy radical 156-176 heme oxygenase 2 Homo sapiens 178-181 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). ro2 193-196 heme oxygenase 2 Homo sapiens 91-94 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). beta-hydroperoxy alkyl radical 249-279 heme oxygenase 2 Homo sapiens 91-94 23829768-1 2013 In this work, we present high-pressure rate rules and branching ratios for the addition of HO2 to olefins through the concerted addition channel to form an alkyl peroxy radical (HO2 + olefin RO2) and through the radical addition channel to form a beta-hydroperoxy alkyl radical (HO2 + olefin beta-QOOH). beta-qooh 296-305 heme oxygenase 2 Homo sapiens 91-94 23829768-5 2013 Next, we calculated apparent pressure- and temperature-dependent rate constants for HO2 addition to the terminal site of 1-butene using an energy-grained master equation (ME) approach and QRRK calculations with a modified strong collision (MSC) approximation. 1-butene 121-129 heme oxygenase 2 Homo sapiens 84-87 23902123-2 2013 Validation and testing were conducted through kinetic measurements of the reaction of HO2 radicals with NO2, and the results were found to be in good agreement with recent recommended values. Nitrogen Dioxide 104-107 heme oxygenase 2 Homo sapiens 86-89 23867390-1 2013 A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2). imidazole 46-55 heme oxygenase 2 Homo sapiens 157-173 23867390-1 2013 A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2). imidazole 46-55 heme oxygenase 2 Homo sapiens 175-179 23822586-0 2013 Hydrogen abstraction from n-butyl formate by H and HO2 . Hydrogen 0-8 heme oxygenase 2 Homo sapiens 52-55 23822586-0 2013 Hydrogen abstraction from n-butyl formate by H and HO2 . BUTYL FORMATE 26-41 heme oxygenase 2 Homo sapiens 52-55 23822586-3 2013 This study reports computed ab initio rates for abstractions by H and HO2 radicals from the recently proposed biofuel candidate n-butyl formate. BUTYL FORMATE 130-145 heme oxygenase 2 Homo sapiens 71-74 23822586-5 2013 Hindered rotation of HO2 with respect to n-butyl formate is treated using accurate eigenvalue summation and shows large influence on the rates. BUTYL FORMATE 42-57 heme oxygenase 2 Homo sapiens 21-24 23822586-7 2013 The abstraction from the gamma carbon by HO2 is slowest, although proceeding over the lowest barriers, due to the important influence of transition state entropies. Carbon 31-37 heme oxygenase 2 Homo sapiens 41-44 23713783-7 2013 Results of the theoretically calculated rate coefficients indicate that the hydrogen abstraction by HO2 from the C2 carbon of both MTHF and DMTHF is the most dominant path among all reaction pathways attributed to its lowest barrier height. Hydrogen 76-84 heme oxygenase 2 Homo sapiens 100-103 23713783-7 2013 Results of the theoretically calculated rate coefficients indicate that the hydrogen abstraction by HO2 from the C2 carbon of both MTHF and DMTHF is the most dominant path among all reaction pathways attributed to its lowest barrier height. Carbon 116-122 heme oxygenase 2 Homo sapiens 100-103 23713783-7 2013 Results of the theoretically calculated rate coefficients indicate that the hydrogen abstraction by HO2 from the C2 carbon of both MTHF and DMTHF is the most dominant path among all reaction pathways attributed to its lowest barrier height. 2-methyltetrahydrofuran 131-135 heme oxygenase 2 Homo sapiens 100-103 23713783-7 2013 Results of the theoretically calculated rate coefficients indicate that the hydrogen abstraction by HO2 from the C2 carbon of both MTHF and DMTHF is the most dominant path among all reaction pathways attributed to its lowest barrier height. 2,5-dimethyltetrahydrofuran 140-145 heme oxygenase 2 Homo sapiens 100-103 23713783-8 2013 The total rate coefficients of the MTHF and DMTHF with HO2 at CCSD(T)/cc-pVTZ//B3LYP/cc-pVTZ level of theory are k(T) = 8.60T(3.54) exp(-8.92/RT) and k(T)= 3.17T(3.63) exp(-6.59/RT) cm(3) mol(-1) s(-1), respectively. 2-methyltetrahydrofuran 35-39 heme oxygenase 2 Homo sapiens 55-58 23713783-8 2013 The total rate coefficients of the MTHF and DMTHF with HO2 at CCSD(T)/cc-pVTZ//B3LYP/cc-pVTZ level of theory are k(T) = 8.60T(3.54) exp(-8.92/RT) and k(T)= 3.17T(3.63) exp(-6.59/RT) cm(3) mol(-1) s(-1), respectively. 2,5-dimethyltetrahydrofuran 44-49 heme oxygenase 2 Homo sapiens 55-58 26283246-2 2013 It is demonstrated that the effect of quantum tunneling corrections for the reaction HO2 + HO2 = H2O2 + O2 can have a noticeable impact on the performance of a high-fidelity model of a compression-ignition (e.g., diesel) engine, and that an accurate prediction of ignition delay time for the engine model requires an accurate estimation of the tunneling correction for this reaction. Hydrogen Peroxide 97-101 heme oxygenase 2 Homo sapiens 91-94 26283246-2 2013 It is demonstrated that the effect of quantum tunneling corrections for the reaction HO2 + HO2 = H2O2 + O2 can have a noticeable impact on the performance of a high-fidelity model of a compression-ignition (e.g., diesel) engine, and that an accurate prediction of ignition delay time for the engine model requires an accurate estimation of the tunneling correction for this reaction. Oxygen 86-88 heme oxygenase 2 Homo sapiens 91-94 23590552-0 2013 Theoretical and kinetic study of the reactions of ketones with HO2 radicals. Ketones 50-57 heme oxygenase 2 Homo sapiens 63-66 23590552-2 2013 This work presents an ab initio and chemical kinetic study of the reaction mechanisms of hydrogen atom abstraction by the HO2 radical on five ketones: dimethyl, ethyl methyl, n-propyl methyl, iso-propyl methyl, and iso-butyl methyl ketones. Hydrogen 89-97 heme oxygenase 2 Homo sapiens 122-125 23590522-0 2013 Theoretical and kinetic study of the reaction of ethyl methyl ketone with HO2 for T = 600-1600 K. Part II: addition reaction channels. methylethyl ketone 49-68 heme oxygenase 2 Homo sapiens 74-77 23590522-1 2013 The temperature and pressure dependence of the addition reaction of ethyl methyl ketone (EMK) with HO2 radical has been calculated using the master equation method employing conventional transition state theory estimates for the microcanonical rate coefficients in the temperature range of 600-1600 K. Geometries, frequencies, and hindrance potentials were obtained at the B3LYP/6-311G(d,p) level of theory. methylethyl ketone 68-87 heme oxygenase 2 Homo sapiens 99-102 23590552-2 2013 This work presents an ab initio and chemical kinetic study of the reaction mechanisms of hydrogen atom abstraction by the HO2 radical on five ketones: dimethyl, ethyl methyl, n-propyl methyl, iso-propyl methyl, and iso-butyl methyl ketones. Ketones 142-149 heme oxygenase 2 Homo sapiens 122-125 23590552-2 2013 This work presents an ab initio and chemical kinetic study of the reaction mechanisms of hydrogen atom abstraction by the HO2 radical on five ketones: dimethyl, ethyl methyl, n-propyl methyl, iso-propyl methyl, and iso-butyl methyl ketones. Ethane 151-159 heme oxygenase 2 Homo sapiens 122-125 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. 1-Buten-2-ol 68-80 heme oxygenase 2 Homo sapiens 83-86 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. 1-Buten-2-ol 68-80 heme oxygenase 2 Homo sapiens 116-119 23590552-2 2013 This work presents an ab initio and chemical kinetic study of the reaction mechanisms of hydrogen atom abstraction by the HO2 radical on five ketones: dimethyl, ethyl methyl, n-propyl methyl, iso-propyl methyl, and iso-butyl methyl ketones. methyl radical 153-159 heme oxygenase 2 Homo sapiens 122-125 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. 2-Buten-2-ol 101-113 heme oxygenase 2 Homo sapiens 116-119 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. Acetic Acid 135-146 heme oxygenase 2 Homo sapiens 83-86 23590552-2 2013 This work presents an ab initio and chemical kinetic study of the reaction mechanisms of hydrogen atom abstraction by the HO2 radical on five ketones: dimethyl, ethyl methyl, n-propyl methyl, iso-propyl methyl, and iso-butyl methyl ketones. methyl radical 167-173 heme oxygenase 2 Homo sapiens 122-125 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. Acetic Acid 135-146 heme oxygenase 2 Homo sapiens 116-119 23590552-2 2013 This work presents an ab initio and chemical kinetic study of the reaction mechanisms of hydrogen atom abstraction by the HO2 radical on five ketones: dimethyl, ethyl methyl, n-propyl methyl, iso-propyl methyl, and iso-butyl methyl ketones. methyl isobutyl ketone 215-239 heme oxygenase 2 Homo sapiens 122-125 23590552-6 2013 The CCSD(T)/cc-pVXZ method (X = D, T, Q) was used for the reaction mechanism of dimethyl ketone + HO2 radical in order to benchmark the computationally less expensive method of CCSD(T)/cc-pVTZ//MP2/6-311G(d,p). Acetone 80-95 heme oxygenase 2 Homo sapiens 98-101 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. ethylene + oh radical 149-170 heme oxygenase 2 Homo sapiens 83-86 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. ethylene + oh radical 149-170 heme oxygenase 2 Homo sapiens 116-119 23560681-4 2013 From the dependences of the time-averaged concentrations for 20 mus of the constituted chemicals on the initial concentration of O3, it was found that the transient spectra involve the decomposition of O3 and the formation of hydrogen peroxide (H2O2) and a third component that is assigned to hydroxyl radical (OH) or perhydroxyl radical (HO2). Ozone 129-131 heme oxygenase 2 Homo sapiens 339-342 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. 2-methyl-2-oxetanol + oh radical 182-214 heme oxygenase 2 Homo sapiens 83-86 23590522-5 2013 Our calculated results show that the four reaction channels forming 1-buten-2-ol + HO2 radical (R5), 2-buten-2-ol + HO2 radical (R10), acetic acid + ethylene + OH radical (R13), and 2-methyl-2-oxetanol + OH radical (R15) are the dominant channels. 2-methyl-2-oxetanol + oh radical 182-214 heme oxygenase 2 Homo sapiens 116-119 23590522-6 2013 When the temperature is below 1000 K, the reaction R15 forming the cyclic ether, 2-methyl-2-oxetanol, is dominant while the reaction R13 forming acetic acid + ethylene + OH radical becomes increasingly dominant at temperatures above 1000 K. The other two channels forming 1-buten-2-ol, 2-buten-2-ol, and HO2 radical are not dominant but are still important product channels over the whole temperature range investigated here. 2-methyl-2-oxetanol 81-100 heme oxygenase 2 Homo sapiens 304-307 23560681-4 2013 From the dependences of the time-averaged concentrations for 20 mus of the constituted chemicals on the initial concentration of O3, it was found that the transient spectra involve the decomposition of O3 and the formation of hydrogen peroxide (H2O2) and a third component that is assigned to hydroxyl radical (OH) or perhydroxyl radical (HO2). Ozone 202-204 heme oxygenase 2 Homo sapiens 339-342 23560681-4 2013 From the dependences of the time-averaged concentrations for 20 mus of the constituted chemicals on the initial concentration of O3, it was found that the transient spectra involve the decomposition of O3 and the formation of hydrogen peroxide (H2O2) and a third component that is assigned to hydroxyl radical (OH) or perhydroxyl radical (HO2). Hydrogen Peroxide 226-243 heme oxygenase 2 Homo sapiens 339-342 23560681-4 2013 From the dependences of the time-averaged concentrations for 20 mus of the constituted chemicals on the initial concentration of O3, it was found that the transient spectra involve the decomposition of O3 and the formation of hydrogen peroxide (H2O2) and a third component that is assigned to hydroxyl radical (OH) or perhydroxyl radical (HO2). Hydrogen Peroxide 245-249 heme oxygenase 2 Homo sapiens 339-342 23560681-6 2013 The time-averaged concentration ratio of each chemical component to the initial O3 concentration depends on the pH conditions from -0.95 to -0.60 for O3, 0.98 to 1.2 for H2O2, 0.002 to 0.29 for OH, and 0.012 to 0.069 for HO2. Ozone 80-82 heme oxygenase 2 Homo sapiens 221-224 22935040-9 2013 The antiproliferative effect of carbon monoxide under stress might decrease the expression of HO-2 under conditions when there is an increasing need for RBC. Carbon Monoxide 32-47 heme oxygenase 2 Homo sapiens 94-98 26291349-1 2013 The first direct in situ measurements of hydroperoxyl radical (HO2) at atmospheric pressure from the exit of a laminar flow reactor have been carried out using mid-infrared Faraday rotation spectroscopy. Hydroperoxy radical 41-61 heme oxygenase 2 Homo sapiens 63-66 26291349-2 2013 HO2 was generated by oxidation of dimethyl ether, a potential renewable biofuel with a simple molecular structure but rich low-temperature oxidation chemistry. dimethyl ether 34-48 heme oxygenase 2 Homo sapiens 0-3 23458562-1 2013 Reaction of methyl radicals with hydroperoxy radicals, CH3 + HO2 products (1) was studied using pulsed laser photolysis coupled to transient UV-vis absorption spectroscopy at 295 K and 1 bar (He). methyl radical 12-27 heme oxygenase 2 Homo sapiens 61-64 23720291-6 2013 The rate-controlling step of heme breakdown is catalyzed by heme oxygenase (HMOX), of which there are two isoforms, called HMOX1 and HMOX2. Heme 29-33 heme oxygenase 2 Homo sapiens 133-138 22923613-0 2012 Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy. Cysteine 8-16 heme oxygenase 2 Homo sapiens 51-67 22923613-0 2012 Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy. Heme 29-33 heme oxygenase 2 Homo sapiens 51-67 22923613-3 2012 HO-2 has three cysteine residues that have been proposed to modulate the affinity for heme, whereas HO-1 has none. Cysteine 15-23 heme oxygenase 2 Homo sapiens 0-4 22923613-3 2012 HO-2 has three cysteine residues that have been proposed to modulate the affinity for heme, whereas HO-1 has none. Heme 86-90 heme oxygenase 2 Homo sapiens 0-4 22923613-4 2012 Here we use site-specific mutagenesis and two-dimensional NMR of l-[3-(13)C]cysteine-labeled proteins to determine the redox state of the individual cysteines in HO-2 and assess their roles in binding of heme. l-[3-(13)c]cysteine 65-84 heme oxygenase 2 Homo sapiens 162-166 22923613-4 2012 Here we use site-specific mutagenesis and two-dimensional NMR of l-[3-(13)C]cysteine-labeled proteins to determine the redox state of the individual cysteines in HO-2 and assess their roles in binding of heme. Cysteine 149-158 heme oxygenase 2 Homo sapiens 162-166 22500669-0 2012 Formation of HO2 radicals from the 248 nm two-photon excitation of different aromatic hydrocarbons in the presence of O2. Hydrocarbons, Aromatic 77-98 heme oxygenase 2 Homo sapiens 13-16 22524792-8 2012 CONCLUSION: the rate-determining step of oxidation in protein backbone is the generation of hydroperoxy peptide radical via the reaction of alkylperoxy peptide radical with HO2. hydroperoxy peptide radical 92-119 heme oxygenase 2 Homo sapiens 173-176 22616859-7 2012 Recent studies with HO2 (haem oxygenase-2), a K+ ion channel (the BK channel) and a nuclear receptor (Rev-Erb) demonstrate that this mode of regulation involves a thiol-disulfide redox switch that regulates haem binding and that gas signalling molecules (CO and NO) modulate the effect of haem. Sulfhydryl Compounds 163-168 heme oxygenase 2 Homo sapiens 20-23 22616859-7 2012 Recent studies with HO2 (haem oxygenase-2), a K+ ion channel (the BK channel) and a nuclear receptor (Rev-Erb) demonstrate that this mode of regulation involves a thiol-disulfide redox switch that regulates haem binding and that gas signalling molecules (CO and NO) modulate the effect of haem. Sulfhydryl Compounds 163-168 heme oxygenase 2 Homo sapiens 25-41 22616859-7 2012 Recent studies with HO2 (haem oxygenase-2), a K+ ion channel (the BK channel) and a nuclear receptor (Rev-Erb) demonstrate that this mode of regulation involves a thiol-disulfide redox switch that regulates haem binding and that gas signalling molecules (CO and NO) modulate the effect of haem. Disulfides 169-178 heme oxygenase 2 Homo sapiens 20-23 22616859-7 2012 Recent studies with HO2 (haem oxygenase-2), a K+ ion channel (the BK channel) and a nuclear receptor (Rev-Erb) demonstrate that this mode of regulation involves a thiol-disulfide redox switch that regulates haem binding and that gas signalling molecules (CO and NO) modulate the effect of haem. Disulfides 169-178 heme oxygenase 2 Homo sapiens 25-41 22431362-5 2012 The compounds with a five-atom linker containing a heteroatom (O or S) were found to be the most potent inhibitors of HO-2; 1-(N-benzylamino)-3-(1H-imidazol-1-yl)propane dihydrochloride, with a nitrogen atom in the linker, was found to be inactive. Nitrogen 194-202 heme oxygenase 2 Homo sapiens 118-122 22524792-8 2012 CONCLUSION: the rate-determining step of oxidation in protein backbone is the generation of hydroperoxy peptide radical via the reaction of alkylperoxy peptide radical with HO2. alkylperoxy peptide radical 140-167 heme oxygenase 2 Homo sapiens 173-176 22524792-9 2012 The stabilities of alkylperoxy peptide radical and complex of alkylperoxy peptide radical with HO2 are crucial in this O-base oxidation reaction. alkylperoxy peptide radical 19-46 heme oxygenase 2 Homo sapiens 95-98 22524792-9 2012 The stabilities of alkylperoxy peptide radical and complex of alkylperoxy peptide radical with HO2 are crucial in this O-base oxidation reaction. alkylperoxy peptide radical 62-89 heme oxygenase 2 Homo sapiens 95-98 22443769-0 2012 A detailed test study of barrier heights for the HO2 + H2O + O3 reaction with various forms of multireference perturbation theory. Water 55-58 heme oxygenase 2 Homo sapiens 49-52 26286401-0 2012 Concerted HO2 Elimination from alpha-Aminoalkylperoxyl Free Radicals: Experimental and Theoretical Evidence from the Gas-Phase NH2( )CHCO2(-) + O2 Reaction. alpha-aminoalkylperoxyl free radicals 31-68 heme oxygenase 2 Homo sapiens 10-13 26286401-0 2012 Concerted HO2 Elimination from alpha-Aminoalkylperoxyl Free Radicals: Experimental and Theoretical Evidence from the Gas-Phase NH2( )CHCO2(-) + O2 Reaction. nh2( )chco2 127-138 heme oxygenase 2 Homo sapiens 10-13 26286401-2 2012 This radical is found to undergo a remarkably rapid reaction with O2 to form the hydroperoxyl radical (HO2( )) and an even-electron imine (NHCHCO2(-)), with experiments and master equation simulations revealing that reaction proceeds at the ion-molecule collision rate. Oxygen 66-68 heme oxygenase 2 Homo sapiens 103-106 26286401-2 2012 This radical is found to undergo a remarkably rapid reaction with O2 to form the hydroperoxyl radical (HO2( )) and an even-electron imine (NHCHCO2(-)), with experiments and master equation simulations revealing that reaction proceeds at the ion-molecule collision rate. Hydroperoxy radical 81-101 heme oxygenase 2 Homo sapiens 103-106 26286401-3 2012 This reaction is facilitated by a low-energy concerted HO2( ) elimination mechanism in the NH2CH(OO( ))CO2(-) peroxyl radical. nh2ch(oo( ))co2(-) peroxyl radical 91-125 heme oxygenase 2 Homo sapiens 55-58 22304481-0 2012 Theoretical determination of the rate coefficient for the HO2 + HO2 H2O2+O2 reaction: adiabatic treatment of anharmonic torsional effects. Hydrogen Peroxide 70-74 heme oxygenase 2 Homo sapiens 58-61 22304481-0 2012 Theoretical determination of the rate coefficient for the HO2 + HO2 H2O2+O2 reaction: adiabatic treatment of anharmonic torsional effects. Hydrogen Peroxide 70-74 heme oxygenase 2 Homo sapiens 64-67 22304481-0 2012 Theoretical determination of the rate coefficient for the HO2 + HO2 H2O2+O2 reaction: adiabatic treatment of anharmonic torsional effects. Oxygen 59-61 heme oxygenase 2 Homo sapiens 64-67 21647550-2 2012 On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences. Iron 253-257 heme oxygenase 2 Homo sapiens 177-193 22006033-0 2011 Water-catalyzed gas-phase hydrogen abstraction reactions of CH3O2 and HO2 with HO2: a computational investigation. Water 0-5 heme oxygenase 2 Homo sapiens 70-73 22006033-0 2011 Water-catalyzed gas-phase hydrogen abstraction reactions of CH3O2 and HO2 with HO2: a computational investigation. Methyldioxy radical 60-65 heme oxygenase 2 Homo sapiens 79-82 25774181-2 2012 Graded concentration and time course experiments demonstrate that curcumin significantly upregulates phosphatidylinositol 3-kinase (PI3K), Akt, nuclear factor E2-related factor-2 (Nrf2), heme oxygenase 1 and ferritin expression, and that it significantly downregulates heme oxygenase 2, reactive oxygen species and amyloid-beta 40/42 expression. Curcumin 66-74 heme oxygenase 2 Homo sapiens 269-285 22006033-0 2011 Water-catalyzed gas-phase hydrogen abstraction reactions of CH3O2 and HO2 with HO2: a computational investigation. Water 0-5 heme oxygenase 2 Homo sapiens 79-82 22006033-0 2011 Water-catalyzed gas-phase hydrogen abstraction reactions of CH3O2 and HO2 with HO2: a computational investigation. Hydrogen 26-34 heme oxygenase 2 Homo sapiens 70-73 22006033-0 2011 Water-catalyzed gas-phase hydrogen abstraction reactions of CH3O2 and HO2 with HO2: a computational investigation. Hydrogen 26-34 heme oxygenase 2 Homo sapiens 79-82 21804464-5 2011 Heme oxygenase-2 is capable of degradation of heme producing free iron ions, thus, diversity in heme oxygenase-2 gene may contribute to AMD. Heme 46-50 heme oxygenase 2 Homo sapiens 0-16 22039914-0 2011 Selective activation of heme oxygenase-2 by menadione. Vitamin K 3 44-53 heme oxygenase 2 Homo sapiens 24-40 22039914-5 2011 This communication describes our observations of the up to 30-fold increase in the in-vitro activation of HO-2 by menadione. Vitamin K 3 114-123 heme oxygenase 2 Homo sapiens 106-110 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Biliverdine 73-83 heme oxygenase 2 Homo sapiens 0-16 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Biliverdine 73-83 heme oxygenase 2 Homo sapiens 18-23 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Iron 100-104 heme oxygenase 2 Homo sapiens 0-16 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Iron 100-104 heme oxygenase 2 Homo sapiens 18-23 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Carbon Monoxide 109-124 heme oxygenase 2 Homo sapiens 0-16 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Carbon Monoxide 109-124 heme oxygenase 2 Homo sapiens 18-23 21701740-2 2011 At 295 K, the isomerization rate of isoprene peroxy radicals (ISO2 ) relative to the rate of reaction of ISO2 + HO2 is k(isom)(295)/(k(ISO2 +HO2)(295)) = (1.2 +- 0.6) x 10(8) mol cm(-3), or k(isom)(295) 0.002 s(-1). isoprene peroxy radicals 36-60 heme oxygenase 2 Homo sapiens 113-116 21701740-2 2011 At 295 K, the isomerization rate of isoprene peroxy radicals (ISO2 ) relative to the rate of reaction of ISO2 + HO2 is k(isom)(295)/(k(ISO2 +HO2)(295)) = (1.2 +- 0.6) x 10(8) mol cm(-3), or k(isom)(295) 0.002 s(-1). isoprene peroxy radicals 36-60 heme oxygenase 2 Homo sapiens 142-145 21804464-5 2011 Heme oxygenase-2 is capable of degradation of heme producing free iron ions, thus, diversity in heme oxygenase-2 gene may contribute to AMD. Heme 46-50 heme oxygenase 2 Homo sapiens 96-112 21804464-5 2011 Heme oxygenase-2 is capable of degradation of heme producing free iron ions, thus, diversity in heme oxygenase-2 gene may contribute to AMD. Iron 66-70 heme oxygenase 2 Homo sapiens 0-16 21804464-5 2011 Heme oxygenase-2 is capable of degradation of heme producing free iron ions, thus, diversity in heme oxygenase-2 gene may contribute to AMD. Iron 66-70 heme oxygenase 2 Homo sapiens 96-112 21787023-0 2011 Quantum chemical analysis of the unfolding of a penta-glycyl 3(10)-helix initiated by HO( ), HO2( ), and O2(- ). penta-glycyl 48-60 heme oxygenase 2 Homo sapiens 93-96 19882733-0 2010 Barrier heights for H-atom abstraction by H*O2 from n-butanol--a simple yet exacting test for model chemistries? 1-Butanol 52-61 heme oxygenase 2 Homo sapiens 42-46 21434683-0 2011 Multichannel RRKM-TST and CVT rate constant calculations for reactions of CH2OH or CH3O with HO2. Hydroxymethyl radical 74-79 heme oxygenase 2 Homo sapiens 93-96 21434683-0 2011 Multichannel RRKM-TST and CVT rate constant calculations for reactions of CH2OH or CH3O with HO2. 7-methoxy-6-(2'-methoxy-3'-hydroxy-3'-methyl butyl) 83-87 heme oxygenase 2 Homo sapiens 93-96 21123734-3 2011 We present novel data that Nox4 NADPH oxidase-derived ROS also initiate a cell survival mechanism by increasing production of a gaseous antioxidant mediator carbon monoxide (CO) by constitutive heme oxygenase-2 (HO-2). Reactive Oxygen Species 54-57 heme oxygenase 2 Homo sapiens 194-210 21123734-3 2011 We present novel data that Nox4 NADPH oxidase-derived ROS also initiate a cell survival mechanism by increasing production of a gaseous antioxidant mediator carbon monoxide (CO) by constitutive heme oxygenase-2 (HO-2). Reactive Oxygen Species 54-57 heme oxygenase 2 Homo sapiens 212-216 21123734-3 2011 We present novel data that Nox4 NADPH oxidase-derived ROS also initiate a cell survival mechanism by increasing production of a gaseous antioxidant mediator carbon monoxide (CO) by constitutive heme oxygenase-2 (HO-2). Carbon Monoxide 157-172 heme oxygenase 2 Homo sapiens 194-210 21123734-3 2011 We present novel data that Nox4 NADPH oxidase-derived ROS also initiate a cell survival mechanism by increasing production of a gaseous antioxidant mediator carbon monoxide (CO) by constitutive heme oxygenase-2 (HO-2). Carbon Monoxide 157-172 heme oxygenase 2 Homo sapiens 212-216 21123734-3 2011 We present novel data that Nox4 NADPH oxidase-derived ROS also initiate a cell survival mechanism by increasing production of a gaseous antioxidant mediator carbon monoxide (CO) by constitutive heme oxygenase-2 (HO-2). Carbon Monoxide 174-176 heme oxygenase 2 Homo sapiens 194-210 21123734-3 2011 We present novel data that Nox4 NADPH oxidase-derived ROS also initiate a cell survival mechanism by increasing production of a gaseous antioxidant mediator carbon monoxide (CO) by constitutive heme oxygenase-2 (HO-2). Carbon Monoxide 174-176 heme oxygenase 2 Homo sapiens 212-216 21174464-0 2011 Kinetics and mechanism of the glyoxal + HO2 reaction: conversion of HO2 to OH by carbonyls. Glyoxal 30-37 heme oxygenase 2 Homo sapiens 40-43 21174464-0 2011 Kinetics and mechanism of the glyoxal + HO2 reaction: conversion of HO2 to OH by carbonyls. Glyoxal 30-37 heme oxygenase 2 Homo sapiens 68-71 20876213-1 2011 HO-2 oxidizes heme to CO and biliverdin; the latter is reduced to bilirubin by biliverdin reductase (BVR). Heme 14-18 heme oxygenase 2 Homo sapiens 0-4 20876213-1 2011 HO-2 oxidizes heme to CO and biliverdin; the latter is reduced to bilirubin by biliverdin reductase (BVR). Carbon Monoxide 22-24 heme oxygenase 2 Homo sapiens 0-4 20876213-1 2011 HO-2 oxidizes heme to CO and biliverdin; the latter is reduced to bilirubin by biliverdin reductase (BVR). Biliverdine 29-39 heme oxygenase 2 Homo sapiens 0-4 20876213-1 2011 HO-2 oxidizes heme to CO and biliverdin; the latter is reduced to bilirubin by biliverdin reductase (BVR). Bilirubin 66-75 heme oxygenase 2 Homo sapiens 0-4 20876213-4 2011 This is the first reporting of regulation of HO-2 by BVR and that their coordinated increase in isolated myocytes and intact heart protects against cardiotoxicity of beta-adrenergic receptor activation by isoproterenol (ISO). Isoproterenol 205-218 heme oxygenase 2 Homo sapiens 45-49 20502928-2 2010 Two heme oxygenase isoforms, HO-1 and HO-2, exist that differ in several ways, including a complete lack of Cys residues in HO-1 and the presence of three Cys residues as part of heme-regulatory motifs (HRMs) in HO-2. Cysteine 108-111 heme oxygenase 2 Homo sapiens 38-42 20502928-2 2010 Two heme oxygenase isoforms, HO-1 and HO-2, exist that differ in several ways, including a complete lack of Cys residues in HO-1 and the presence of three Cys residues as part of heme-regulatory motifs (HRMs) in HO-2. Cysteine 155-158 heme oxygenase 2 Homo sapiens 38-42 20502928-3 2010 HRMs in other heme proteins are thought to directly bind heme, or to otherwise regulate protein stability or activity; however, it is not currently known how the HRMs exert these effects on HO-2 function. Heme 14-18 heme oxygenase 2 Homo sapiens 190-194 20502928-6 2010 Absorption and magnetic circular dichroism spectroscopic data of these HO-2 variants clearly demonstrate that a new low-spin Fe(III) heme species characteristic of thiolate ligation is formed when Cys265 is reduced. fe(iii) heme 125-137 heme oxygenase 2 Homo sapiens 71-75 20502928-6 2010 Absorption and magnetic circular dichroism spectroscopic data of these HO-2 variants clearly demonstrate that a new low-spin Fe(III) heme species characteristic of thiolate ligation is formed when Cys265 is reduced. thiolate 164-172 heme oxygenase 2 Homo sapiens 71-75 20502928-7 2010 Additionally, absorption, magnetic circular dichroism, and resonance Raman data collected at different temperatures reveal an intriguing temperature dependence of the iron spin state in the heme-HO-2 complex. Iron 167-171 heme oxygenase 2 Homo sapiens 195-199 20502928-8 2010 These findings are consistent with the presence of a hydrogen-bonding network at the heme"s distal side within the active site of HO-2 with potentially significant differences from that observed in HO-1. Hydrogen 53-61 heme oxygenase 2 Homo sapiens 130-134 20502928-8 2010 These findings are consistent with the presence of a hydrogen-bonding network at the heme"s distal side within the active site of HO-2 with potentially significant differences from that observed in HO-1. Heme 85-89 heme oxygenase 2 Homo sapiens 130-134 20524693-5 2010 The C2H5O2 self-reaction is complicated by secondary production of HO2. c2h5o2 4-10 heme oxygenase 2 Homo sapiens 67-70 20812781-5 2011 We review recent results that define a mechanism for how thiol/disulfide redox switches that control heme binding can regulate the activities of an enzyme, heme oxygenase-2, and an ion channel, the BK potassium channel. Sulfhydryl Compounds 57-62 heme oxygenase 2 Homo sapiens 156-172 20812781-5 2011 We review recent results that define a mechanism for how thiol/disulfide redox switches that control heme binding can regulate the activities of an enzyme, heme oxygenase-2, and an ion channel, the BK potassium channel. Disulfides 63-72 heme oxygenase 2 Homo sapiens 156-172 20812781-5 2011 We review recent results that define a mechanism for how thiol/disulfide redox switches that control heme binding can regulate the activities of an enzyme, heme oxygenase-2, and an ion channel, the BK potassium channel. Heme 101-105 heme oxygenase 2 Homo sapiens 156-172 20812781-7 2011 Finally, a model is proposed to describe how the redox switches on heme oxygenase-2 and the BK channel form an interconnected system that is poised to sense oxygen levels in the bloodstream and to elicit the hypoxic response when oxygen levels drop below a threshold value. Oxygen 157-163 heme oxygenase 2 Homo sapiens 67-83 21765894-6 2011 Surprisingly, HO-2 expression was inhibited upon incubation with heme. Heme 65-69 heme oxygenase 2 Homo sapiens 14-18 20979084-0 2010 HO2 formation from the photoexcitation of benzene/O2 mixtures at 248 nm: an energy dependence study. Benzene 42-49 heme oxygenase 2 Homo sapiens 0-3 20807546-0 2010 Carbon monoxide derived from heme oxygenase-2 mediates reduction of methylmercury toxicity in SH-SY5Y cells. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 29-45 20427280-3 2010 Furthermore, evidence suggests that human heme oxygenase-2 (HO2) acts as an oxygen sensor and CO donor that can form a protein complex with the BK channel. Oxygen 47-53 heme oxygenase 2 Homo sapiens 60-63 20427280-4 2010 Here we describe a thiol/disulfide redox switch in the human BK channel and biochemical experiments of heme, CO, and HO2 binding to a 134-residue region within the cytoplasmic domain of the channel. Disulfides 25-34 heme oxygenase 2 Homo sapiens 117-120 20392098-0 2010 Experimental study of the rate of OH + HO2 --> H2O + O2 at high temperatures using the reverse reaction. Water 50-53 heme oxygenase 2 Homo sapiens 39-42 19780600-0 2009 Water vapor effect on the HNO3 yield in the HO2 + NO reaction: experimental and theoretical evidence. Water 0-5 heme oxygenase 2 Homo sapiens 44-47 19943615-6 2010 In forested environments reaction of the beta-hydroxyperoxy radicals with HO2 is expected to dominate, with a small contribution from the mechanism described here. beta-hydroxyperoxy radicals 41-68 heme oxygenase 2 Homo sapiens 74-77 20617734-1 2010 Hydrogen peroxide is not only an important oxidant in itself; it also serves as both sink and temporary reservoir for other important oxidants including HOx (OH and HO2) radicals and O3 in the atmosphere. Hydrogen Peroxide 0-17 heme oxygenase 2 Homo sapiens 165-168 20118244-9 2010 These data indicate that HO-2 is important in maintaining endothelial viability and may preserve local regulation of vascular tone, thrombosis, and inflammatory responses during reductions in systemic oxygen delivery. Oxygen 201-207 heme oxygenase 2 Homo sapiens 25-29 26602503-9 2009 Thermal decomposition of benzyl hydroperoxide, formed by hydrogen abstraction reactions in the benzylperoxy radical and at low temperatures in the benzylperoxy + H and benzyl + HO2 reactions, is also investigated. Benzyl hydroperoxide 25-45 heme oxygenase 2 Homo sapiens 177-180 26602503-9 2009 Thermal decomposition of benzyl hydroperoxide, formed by hydrogen abstraction reactions in the benzylperoxy radical and at low temperatures in the benzylperoxy + H and benzyl + HO2 reactions, is also investigated. Hydrogen 57-65 heme oxygenase 2 Homo sapiens 177-180 19780600-0 2009 Water vapor effect on the HNO3 yield in the HO2 + NO reaction: experimental and theoretical evidence. Nitric Acid 26-30 heme oxygenase 2 Homo sapiens 44-47 19694439-4 2009 In this study, we have examined the equilibrium binding of three isocyanides, isopropyl, n-butyl, and benzyl, to the two major human HO isoforms (hHO-1 and hHO-2), Candida albicans HO (CaHmx1), and human cytochrome P450 CYP3A4 using electronic absorption spectroscopy. Cyanides 65-76 heme oxygenase 2 Homo sapiens 156-161 19727497-0 2009 Laboratory study of the interaction of HO2 radicals with the NaCl, NaBr, MgCl(2).6H2O and sea salt surfaces. Sodium Chloride 61-65 heme oxygenase 2 Homo sapiens 39-42 19727497-0 2009 Laboratory study of the interaction of HO2 radicals with the NaCl, NaBr, MgCl(2).6H2O and sea salt surfaces. sodium bromide 67-71 heme oxygenase 2 Homo sapiens 39-42 19727497-0 2009 Laboratory study of the interaction of HO2 radicals with the NaCl, NaBr, MgCl(2).6H2O and sea salt surfaces. Magnesium Chloride 73-85 heme oxygenase 2 Homo sapiens 39-42 19727497-1 2009 The uptake of HO2 radicals on synthetic sea salt, NaCl, NaBr and MgCl(2).6H2O dry solid films was studied over the temperature range 240 to 340 K and at 1 Torr pressure of helium using a discharge flow reactor coupled to a modulated molecular beam mass spectrometer. Salts 44-48 heme oxygenase 2 Homo sapiens 14-17 19727497-1 2009 The uptake of HO2 radicals on synthetic sea salt, NaCl, NaBr and MgCl(2).6H2O dry solid films was studied over the temperature range 240 to 340 K and at 1 Torr pressure of helium using a discharge flow reactor coupled to a modulated molecular beam mass spectrometer. Sodium Chloride 50-54 heme oxygenase 2 Homo sapiens 14-17 19727497-1 2009 The uptake of HO2 radicals on synthetic sea salt, NaCl, NaBr and MgCl(2).6H2O dry solid films was studied over the temperature range 240 to 340 K and at 1 Torr pressure of helium using a discharge flow reactor coupled to a modulated molecular beam mass spectrometer. sodium bromide 56-60 heme oxygenase 2 Homo sapiens 14-17 19727497-1 2009 The uptake of HO2 radicals on synthetic sea salt, NaCl, NaBr and MgCl(2).6H2O dry solid films was studied over the temperature range 240 to 340 K and at 1 Torr pressure of helium using a discharge flow reactor coupled to a modulated molecular beam mass spectrometer. Magnesium Chloride 65-77 heme oxygenase 2 Homo sapiens 14-17 19727497-1 2009 The uptake of HO2 radicals on synthetic sea salt, NaCl, NaBr and MgCl(2).6H2O dry solid films was studied over the temperature range 240 to 340 K and at 1 Torr pressure of helium using a discharge flow reactor coupled to a modulated molecular beam mass spectrometer. Helium 172-178 heme oxygenase 2 Homo sapiens 14-17 19727497-3 2009 H2O2 was observed as a main product of HO2 interaction with salt surface indicating a heterogeneous HO2 self reaction mechanism. Hydrogen Peroxide 0-4 heme oxygenase 2 Homo sapiens 39-42 19727497-3 2009 H2O2 was observed as a main product of HO2 interaction with salt surface indicating a heterogeneous HO2 self reaction mechanism. Hydrogen Peroxide 0-4 heme oxygenase 2 Homo sapiens 100-103 19727497-4 2009 The results show that the HO2 loss through heterogeneous interaction with salt surface is not sufficiently rapid to explain the observed differences between modeled and measured HO2 concentrations in remote coastal areas. Salts 74-78 heme oxygenase 2 Homo sapiens 26-29 19694477-0 2009 Theoretical study on reactions of HO2 radical with photodissociation products of Cl2SO (ClSO and SO). cl2so 81-86 heme oxygenase 2 Homo sapiens 34-37 19694477-0 2009 Theoretical study on reactions of HO2 radical with photodissociation products of Cl2SO (ClSO and SO). clso 88-92 heme oxygenase 2 Homo sapiens 34-37 19694477-1 2009 The possible reactions of HO2 radical with the intermediates of the Cl2SO photolysis (ClSO and SO) were studied using G3MP2//B3LYP/cc-pVTZ+d level of theory and Martin"s W1U method. cl2so 68-73 heme oxygenase 2 Homo sapiens 26-29 19694477-1 2009 The possible reactions of HO2 radical with the intermediates of the Cl2SO photolysis (ClSO and SO) were studied using G3MP2//B3LYP/cc-pVTZ+d level of theory and Martin"s W1U method. clso 86-90 heme oxygenase 2 Homo sapiens 26-29 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 33-37 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 33-37 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 33-37 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. perhydroxyl radical 138-141 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. perhydroxyl radical 138-141 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. perhydroxyl radical 138-141 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. oh + clso2 173-183 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. oh + clso2 173-183 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. oh + clso2 173-183 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. Sulfur Dioxide 180-183 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. Sulfur Dioxide 180-183 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. Sulfur Dioxide 180-183 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. clso 125-129 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. oh + clso2 260-270 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. oh + clso2 260-270 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. oh + clso2 260-270 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. Sulfur Dioxide 201-204 heme oxygenase 2 Homo sapiens 25-28 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. Sulfur Dioxide 201-204 heme oxygenase 2 Homo sapiens 119-122 19694477-2 2009 For the reaction between HO2 and ClSO radicals, the following mechanisms are supposed to be the main reaction pathways HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO + Cl + SO2, HO2 + ClSO --> 3HOO x ClSO --> HOO(Cl)SO --> OH + ClSO2 --> HO(Cl)SO2. Sulfur Dioxide 201-204 heme oxygenase 2 Homo sapiens 119-122 19694477-3 2009 On the basis of G3MP2//B3LYP/cc-pVTZ+d and highly accurate W1U calculations, the reaction of HOO with 3SO species has also been explored, and the following dominant consecutive reactions may describe the fast oxygen transfer HO2 + 3SO --> 4HOO x SO --> 2HOOSO --> OH + SO2. perhydroxyl radical 93-96 heme oxygenase 2 Homo sapiens 225-228 19694477-3 2009 On the basis of G3MP2//B3LYP/cc-pVTZ+d and highly accurate W1U calculations, the reaction of HOO with 3SO species has also been explored, and the following dominant consecutive reactions may describe the fast oxygen transfer HO2 + 3SO --> 4HOO x SO --> 2HOOSO --> OH + SO2. Oxygen 209-215 heme oxygenase 2 Homo sapiens 225-228 19694477-3 2009 On the basis of G3MP2//B3LYP/cc-pVTZ+d and highly accurate W1U calculations, the reaction of HOO with 3SO species has also been explored, and the following dominant consecutive reactions may describe the fast oxygen transfer HO2 + 3SO --> 4HOO x SO --> 2HOOSO --> OH + SO2. oh + so2 273-281 heme oxygenase 2 Homo sapiens 225-228 19694477-6 2009 In the case of the ClSO and HO2 reaction, the dissociation of HOO(Cl)SO resulted in OH and ClSO2. clso 19-23 heme oxygenase 2 Homo sapiens 28-31 19694477-6 2009 In the case of the ClSO and HO2 reaction, the dissociation of HOO(Cl)SO resulted in OH and ClSO2. perhydroxyl radical 62-65 heme oxygenase 2 Homo sapiens 28-31 19694477-6 2009 In the case of the ClSO and HO2 reaction, the dissociation of HOO(Cl)SO resulted in OH and ClSO2. clso2 91-96 heme oxygenase 2 Homo sapiens 28-31 19473966-0 2009 Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. Heme 0-4 heme oxygenase 2 Homo sapiens 26-42 19473966-0 2009 Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. Sulfhydryl Compounds 50-55 heme oxygenase 2 Homo sapiens 26-42 19473966-0 2009 Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. Disulfides 56-65 heme oxygenase 2 Homo sapiens 26-42 19473966-4 2009 Unlike HO-1, which lacks cysteine residues, HO-2 contains three Cys-Pro signatures, known as heme regulatory motifs (HRMs), which are known to control processes related to iron and oxidative metabolism in organisms from bacteria to humans. Cysteine 25-33 heme oxygenase 2 Homo sapiens 44-48 19473966-4 2009 Unlike HO-1, which lacks cysteine residues, HO-2 contains three Cys-Pro signatures, known as heme regulatory motifs (HRMs), which are known to control processes related to iron and oxidative metabolism in organisms from bacteria to humans. Cysteine 64-67 heme oxygenase 2 Homo sapiens 44-48 19473966-4 2009 Unlike HO-1, which lacks cysteine residues, HO-2 contains three Cys-Pro signatures, known as heme regulatory motifs (HRMs), which are known to control processes related to iron and oxidative metabolism in organisms from bacteria to humans. Proline 68-71 heme oxygenase 2 Homo sapiens 44-48 19473966-4 2009 Unlike HO-1, which lacks cysteine residues, HO-2 contains three Cys-Pro signatures, known as heme regulatory motifs (HRMs), which are known to control processes related to iron and oxidative metabolism in organisms from bacteria to humans. Heme 93-97 heme oxygenase 2 Homo sapiens 44-48 19473966-4 2009 Unlike HO-1, which lacks cysteine residues, HO-2 contains three Cys-Pro signatures, known as heme regulatory motifs (HRMs), which are known to control processes related to iron and oxidative metabolism in organisms from bacteria to humans. Iron 172-176 heme oxygenase 2 Homo sapiens 44-48 19473966-5 2009 In HO-2, the C-terminal HRMs constitute a thiol/disulfide redox switch that regulates affinity of the enzyme for heme (Yi, L., and Ragsdale, S. W. (2007) J. Biol. Sulfhydryl Compounds 42-47 heme oxygenase 2 Homo sapiens 3-7 19473966-5 2009 In HO-2, the C-terminal HRMs constitute a thiol/disulfide redox switch that regulates affinity of the enzyme for heme (Yi, L., and Ragsdale, S. W. (2007) J. Biol. Disulfides 48-57 heme oxygenase 2 Homo sapiens 3-7 19473966-5 2009 In HO-2, the C-terminal HRMs constitute a thiol/disulfide redox switch that regulates affinity of the enzyme for heme (Yi, L., and Ragsdale, S. W. (2007) J. Biol. Heme 113-117 heme oxygenase 2 Homo sapiens 3-7 19473966-8 2009 Here, we demonstrate that the thiol/disulfide switch in human HO-2 is physiologically relevant. Sulfhydryl Compounds 30-35 heme oxygenase 2 Homo sapiens 62-66 19473966-8 2009 Here, we demonstrate that the thiol/disulfide switch in human HO-2 is physiologically relevant. Disulfides 36-45 heme oxygenase 2 Homo sapiens 62-66 19473966-13 2009 Thus, the thiol/disulfide switch in HO-2 responds to cellular oxidative stress and reductive conditions, representing a paradigm for how HRMs can integrate heme homeostasis with CO signaling and redox regulation of cellular metabolism. Sulfhydryl Compounds 10-15 heme oxygenase 2 Homo sapiens 36-40 19473966-13 2009 Thus, the thiol/disulfide switch in HO-2 responds to cellular oxidative stress and reductive conditions, representing a paradigm for how HRMs can integrate heme homeostasis with CO signaling and redox regulation of cellular metabolism. Disulfides 16-25 heme oxygenase 2 Homo sapiens 36-40 19220039-6 2009 Whereas the hydrogen abstraction reaction producing S + HO2 is found to proceed on the quartet surface, the substantial barrier of approximately 165 kJ mol-1 means that it occurs as a minor product channel. Hydrogen 12-20 heme oxygenase 2 Homo sapiens 56-59 19106038-1 2009 Nitric oxide and carbon monoxide are diffusible gas messengers, synthesized by nitric oxide synthase or heme oxygenase 2, respectively, that can activate soluble guanylyl cyclase in adjacent cells. Nitric Oxide 0-12 heme oxygenase 2 Homo sapiens 104-120 19106038-1 2009 Nitric oxide and carbon monoxide are diffusible gas messengers, synthesized by nitric oxide synthase or heme oxygenase 2, respectively, that can activate soluble guanylyl cyclase in adjacent cells. Carbon Monoxide 17-32 heme oxygenase 2 Homo sapiens 104-120 19536469-2 2009 It has recently been proposed that hypoxic inhibition involves either activation of AMP activated protein kinase (AMPK) or inhibition of carbon monoxide (CO) production by heme oxygenase 2 (HO-2). Carbon Monoxide 137-152 heme oxygenase 2 Homo sapiens 172-188 19238980-1 2009 The role of primary active species (ecb(-), hvb(+), *OH, HO2*, O2*(-), and H2O2) during photocatalytic degradation of paracetamol (acetaminophen) using TiO2 catalyst was systematically investigated. Acetaminophen 118-129 heme oxygenase 2 Homo sapiens 57-60 19536501-5 2009 The cellular and molecular mechanisms of acute O(2)-sensing in the brain remain to be determined but they appear to involve O(2)-sensitive ion channels and heme oxygenase-2, which acts by a different mechanism than has been described for the carotid body. Oxygen 47-51 heme oxygenase 2 Homo sapiens 156-172 19536469-2 2009 It has recently been proposed that hypoxic inhibition involves either activation of AMP activated protein kinase (AMPK) or inhibition of carbon monoxide (CO) production by heme oxygenase 2 (HO-2). Carbon Monoxide 154-157 heme oxygenase 2 Homo sapiens 172-188 23675099-4 2008 Approximately 0.3% of O2 ( -) present in cytosol exists in its protonated form: hydroperoxyl radical (HO2 ( )). Superoxides 22-24 heme oxygenase 2 Homo sapiens 102-105 23675099-4 2008 Approximately 0.3% of O2 ( -) present in cytosol exists in its protonated form: hydroperoxyl radical (HO2 ( )). Hydroperoxy radical 80-100 heme oxygenase 2 Homo sapiens 102-105 18226911-5 2008 We found that O(2) addition to the (preferentially deprotonated) pyrrole substrate (yielding a hydroperoxide, which then abstracts a proton from the reactive propionate substituent) is compatible with the observed experimental reaction rate, and that the reaction may then proceed through HO2- elimination, followed by decarboxylation. Oxygen 14-18 heme oxygenase 2 Homo sapiens 289-292 18707179-0 2008 The effects of water vapor on the CH3O2 self-reaction and reaction with HO2. Water 15-20 heme oxygenase 2 Homo sapiens 72-75 18707179-3 2008 The HO2 self-reaction rate constant is significantly enhanced by water vapor, consistent with what others have reported, whereas the CH3O2 self-reaction and the cross-reaction (CH3O2 + HO2) rate constants are nearly unaffected. Water 65-70 heme oxygenase 2 Homo sapiens 4-7 18707179-4 2008 The enhancement in the HO2 self-reaction rate coefficient occurs because of the formation of a strongly bound (6.9 kcal mol(-1)) HO2 x H2O complex during the reaction mechanism where the H2O acts as an energy chaperone. Water 135-138 heme oxygenase 2 Homo sapiens 23-26 18707179-4 2008 The enhancement in the HO2 self-reaction rate coefficient occurs because of the formation of a strongly bound (6.9 kcal mol(-1)) HO2 x H2O complex during the reaction mechanism where the H2O acts as an energy chaperone. Water 135-138 heme oxygenase 2 Homo sapiens 129-132 18707179-4 2008 The enhancement in the HO2 self-reaction rate coefficient occurs because of the formation of a strongly bound (6.9 kcal mol(-1)) HO2 x H2O complex during the reaction mechanism where the H2O acts as an energy chaperone. Water 187-190 heme oxygenase 2 Homo sapiens 23-26 18707179-4 2008 The enhancement in the HO2 self-reaction rate coefficient occurs because of the formation of a strongly bound (6.9 kcal mol(-1)) HO2 x H2O complex during the reaction mechanism where the H2O acts as an energy chaperone. Water 187-190 heme oxygenase 2 Homo sapiens 129-132 18767648-7 2008 The water effect seems to be influenced by the HO2/RO2 ratio. Water 4-9 heme oxygenase 2 Homo sapiens 47-50 18412543-1 2008 hBVR (human biliverdin reductase) is an enzyme that reduces biliverdin (the product of haem oxygenases HO-1 and HO-2 activity) to the antioxidant bilirubin. Biliverdine 12-22 heme oxygenase 2 Homo sapiens 87-116 18412543-1 2008 hBVR (human biliverdin reductase) is an enzyme that reduces biliverdin (the product of haem oxygenases HO-1 and HO-2 activity) to the antioxidant bilirubin. Bilirubin 146-155 heme oxygenase 2 Homo sapiens 87-116 18491883-0 2008 The temperature and pressure dependence of the reactions H + O2 (+M) --> HO2 (+M) and H + OH (+M) --> H2O (+M). perhydroxyl radical 57-63 heme oxygenase 2 Homo sapiens 76-79 18491883-1 2008 The reactions H + O2 (+M) --> HO2 (+M) and H + OH (+M) --> H2O (+M) have been studied using high-level quantum chemistry methods. perhydroxyl radical 14-20 heme oxygenase 2 Homo sapiens 33-36 18454512-3 2008 This is contrary to previous findings of HO2 radical interactions with water clusters. Water 71-76 heme oxygenase 2 Homo sapiens 41-44 18454512-4 2008 Natural bond orbital (NBO) analysis is used to analyze the bonding feature of OH to help explain the difference in behavior between OH and HO2 radicals toward a water surface. Water 161-166 heme oxygenase 2 Homo sapiens 139-142 18288821-0 2008 Kinetics of heterogeneous reactions of HO2 radical at ambient concentration levels with (NH4)2SO4 and NaCl aerosol particles. Ammonium Sulfate 88-97 heme oxygenase 2 Homo sapiens 39-42 18288821-0 2008 Kinetics of heterogeneous reactions of HO2 radical at ambient concentration levels with (NH4)2SO4 and NaCl aerosol particles. Sodium Chloride 102-106 heme oxygenase 2 Homo sapiens 39-42 18288821-1 2008 The HO2 uptake coefficient (gamma) for inorganic submicrometer wet and dry aerosol particles ((NH4)2SO4 and NaCl) under ambient conditions (760 Torr and 296 +/- 2 K) was measured using an aerosol flow tube (AFT) coupled with a chemical conversion/laser-induced fluorescence (CC/LIF) technique. Ammonium Sulfate 94-103 heme oxygenase 2 Homo sapiens 4-7 18288821-1 2008 The HO2 uptake coefficient (gamma) for inorganic submicrometer wet and dry aerosol particles ((NH4)2SO4 and NaCl) under ambient conditions (760 Torr and 296 +/- 2 K) was measured using an aerosol flow tube (AFT) coupled with a chemical conversion/laser-induced fluorescence (CC/LIF) technique. Sodium Chloride 108-112 heme oxygenase 2 Homo sapiens 4-7 18226911-5 2008 We found that O(2) addition to the (preferentially deprotonated) pyrrole substrate (yielding a hydroperoxide, which then abstracts a proton from the reactive propionate substituent) is compatible with the observed experimental reaction rate, and that the reaction may then proceed through HO2- elimination, followed by decarboxylation. Pyrroles 65-72 heme oxygenase 2 Homo sapiens 289-292 18226911-5 2008 We found that O(2) addition to the (preferentially deprotonated) pyrrole substrate (yielding a hydroperoxide, which then abstracts a proton from the reactive propionate substituent) is compatible with the observed experimental reaction rate, and that the reaction may then proceed through HO2- elimination, followed by decarboxylation. Hydrogen Peroxide 95-108 heme oxygenase 2 Homo sapiens 289-292 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Carbon Monoxide 131-146 heme oxygenase 2 Homo sapiens 116-120 18315954-0 2008 Protective effect of p53 in vascular smooth muscle cells against nitric oxide-induced apoptosis is mediated by up-regulation of heme oxygenase-2. Nitric Oxide 65-77 heme oxygenase 2 Homo sapiens 128-144 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Heme 12-16 heme oxygenase 2 Homo sapiens 116-120 18266341-1 2008 The uptake of trace gases such as OH and HO2 radicals, NH3, ClONO2, N2O5, ozone, and many other gases by water, aqueous solutions of acids, and salts has been reported by numerous investigators using a variety of techniques. Water 105-110 heme oxygenase 2 Homo sapiens 41-44 18266341-7 2008 Uptake coefficients for OH and HO2 radicals on water in wetted-wall tubes are shown to range from 0.01 to 1, and on sulfuric acid, they vary from 0.008 to 0.03. Water 47-52 heme oxygenase 2 Homo sapiens 31-34 18289071-4 2008 Pharmacological inhibition or gene deletion of brain HO-2 exacerbates oxidative stress induced by seizures, glutamate, and inflammatory cytokines, and causes cerebral vascular injury. Glutamic Acid 108-117 heme oxygenase 2 Homo sapiens 53-57 17965015-0 2007 Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. Heme 23-27 heme oxygenase 2 Homo sapiens 74-90 17965015-2 2007 The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Heme 35-39 heme oxygenase 2 Homo sapiens 62-66 17965015-3 2007 Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. Heme 22-26 heme oxygenase 2 Homo sapiens 30-34 17965015-3 2007 Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. alpha-mesocarbon 87-103 heme oxygenase 2 Homo sapiens 30-34 17965015-8 2007 The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions. Heme 37-41 heme oxygenase 2 Homo sapiens 48-52 17965015-8 2007 The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions. Heme 37-41 heme oxygenase 2 Homo sapiens 70-74 17965015-8 2007 The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions. Heme 98-102 heme oxygenase 2 Homo sapiens 48-52 17965015-8 2007 The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions. Heme 98-102 heme oxygenase 2 Homo sapiens 70-74 18061915-6 2007 The very fast benzyl peroxyl-initiated co-oxidation of benzyl alcohol generates HO2* radicals, along with benzaldehyde. Benzyl Alcohol 55-69 heme oxygenase 2 Homo sapiens 80-83 18061915-7 2007 This reaction also causes a decrease in the overall oxidation rate, due to the fast chain-terminating reaction of HO2*with the benzylperoxyl radicals, which causes a loss of chain carriers. benzylperoxyl radicals 127-149 heme oxygenase 2 Homo sapiens 114-117 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. phch2ooh 38-46 heme oxygenase 2 Homo sapiens 208-211 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. Hydrogen Peroxide 94-98 heme oxygenase 2 Homo sapiens 47-50 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. Hydrogen Peroxide 94-98 heme oxygenase 2 Homo sapiens 208-211 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. Hydrogen Peroxide 133-137 heme oxygenase 2 Homo sapiens 208-211 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. phch2ooh 150-158 heme oxygenase 2 Homo sapiens 47-50 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. phch2ooh 150-158 heme oxygenase 2 Homo sapiens 208-211 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. Alcohols 189-196 heme oxygenase 2 Homo sapiens 47-50 18061915-8 2007 Moreover, due to the fast equilibrium PhCH2OOH+HO2* right harpoon over left harpoonPhCH2OO* + H2O2, and the much lower reactivity of H2O2 compared to PhCH2OOH, the fast co-oxidation of the alcohol means that HO2* gradually takes over the role of benzylperoxyl as principal chain carrier. Alcohols 189-196 heme oxygenase 2 Homo sapiens 208-211 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Iron 148-152 heme oxygenase 2 Homo sapiens 116-120 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Biliverdine 158-168 heme oxygenase 2 Homo sapiens 116-120 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Bilirubin 196-205 heme oxygenase 2 Homo sapiens 116-120 17887916-5 2007 Characteristically, human HO-1 contains no Cys residue, whereas human HO-2 contains three Cys residues, each of which might be involved in heme binding. Cysteine 90-93 heme oxygenase 2 Homo sapiens 70-74 17887916-5 2007 Characteristically, human HO-1 contains no Cys residue, whereas human HO-2 contains three Cys residues, each of which might be involved in heme binding. Heme 139-143 heme oxygenase 2 Homo sapiens 70-74 17937289-8 2007 Four product pathways are energetically feasible for DDVP degradation initiated by OH radicals in the atmosphere and are consistent with the experimentally observed products CCl2O and CO, but the additional products CCl2CHO, (CH3O)2P(O)OH, HO2, and a closed-shell organophosphorus compound denoted P10 are also predicted. oh radicals 83-94 heme oxygenase 2 Homo sapiens 240-243 18044519-4 2007 The experiments with elevated HO2 levels indicate that organic hydroperoxide compounds should contribute to SOA formation. Hydrogen Peroxide 63-76 heme oxygenase 2 Homo sapiens 30-33 18044519-5 2007 Nitrogen oxide (NO) is shown to reduce aerosol formation; the constant aerosol formation rate obtained before addition of NO and after consumption of NO strongly suggests that aerosol formation is mainlythrough reactions with OH and HO2 radicals. Nitrogen Oxides 0-14 heme oxygenase 2 Homo sapiens 233-236 17845014-1 2007 Nitrones are potential synthetic antioxidants against the reduction of radical-mediated oxidative damage in cells and as analytical reagents for the identification of HO2* and other such transient species. nitrones 0-8 heme oxygenase 2 Homo sapiens 167-170 17845014-4 2007 The trend in HO2* reactivity to nitrones could not be explained solely on the basis of the relationship of the theoretical positive charge densities on the nitronyl-C, with their respective ionization potentials, electron affinities, rate constants, or free energies of reaction. nitrones 32-40 heme oxygenase 2 Homo sapiens 13-16 17845014-4 2007 The trend in HO2* reactivity to nitrones could not be explained solely on the basis of the relationship of the theoretical positive charge densities on the nitronyl-C, with their respective ionization potentials, electron affinities, rate constants, or free energies of reaction. nitronyl-c 156-166 heme oxygenase 2 Homo sapiens 13-16 17845014-5 2007 However, various modes of intramolecular H-bonding interaction were observed at the transition state (TS) structures of HO2* addition to nitrones. nitrones 137-145 heme oxygenase 2 Homo sapiens 120-123 17845014-7 2007 In general, HO2* addition to ethoxycarbonyl- and spirolactam-substituted nitrones, as well as those nitrones without electron-withdrawing substituents, such as 5,5-dimethyl-pyrroline N-oxide (DMPO) and 5-spirocyclopentyl-pyrroline N-oxide (CPPO), are most preferred compared to the methylcarbamoyl-substituted nitrones. ethoxycarbonyl- and spirolactam-substituted nitrones 29-81 heme oxygenase 2 Homo sapiens 12-15 17845014-7 2007 In general, HO2* addition to ethoxycarbonyl- and spirolactam-substituted nitrones, as well as those nitrones without electron-withdrawing substituents, such as 5,5-dimethyl-pyrroline N-oxide (DMPO) and 5-spirocyclopentyl-pyrroline N-oxide (CPPO), are most preferred compared to the methylcarbamoyl-substituted nitrones. nitrones 73-81 heme oxygenase 2 Homo sapiens 12-15 17845014-7 2007 In general, HO2* addition to ethoxycarbonyl- and spirolactam-substituted nitrones, as well as those nitrones without electron-withdrawing substituents, such as 5,5-dimethyl-pyrroline N-oxide (DMPO) and 5-spirocyclopentyl-pyrroline N-oxide (CPPO), are most preferred compared to the methylcarbamoyl-substituted nitrones. 5,5-dimethyl-pyrroline N-oxide 192-196 heme oxygenase 2 Homo sapiens 12-15 17845014-7 2007 In general, HO2* addition to ethoxycarbonyl- and spirolactam-substituted nitrones, as well as those nitrones without electron-withdrawing substituents, such as 5,5-dimethyl-pyrroline N-oxide (DMPO) and 5-spirocyclopentyl-pyrroline N-oxide (CPPO), are most preferred compared to the methylcarbamoyl-substituted nitrones. 5-spirocyclopentyl-pyrroline n-oxide 202-238 heme oxygenase 2 Homo sapiens 12-15 17845014-7 2007 In general, HO2* addition to ethoxycarbonyl- and spirolactam-substituted nitrones, as well as those nitrones without electron-withdrawing substituents, such as 5,5-dimethyl-pyrroline N-oxide (DMPO) and 5-spirocyclopentyl-pyrroline N-oxide (CPPO), are most preferred compared to the methylcarbamoyl-substituted nitrones. bis(2,4,5-trichloro-6-carbopentoxyphenyl)oxalate 240-244 heme oxygenase 2 Homo sapiens 12-15 17845014-7 2007 In general, HO2* addition to ethoxycarbonyl- and spirolactam-substituted nitrones, as well as those nitrones without electron-withdrawing substituents, such as 5,5-dimethyl-pyrroline N-oxide (DMPO) and 5-spirocyclopentyl-pyrroline N-oxide (CPPO), are most preferred compared to the methylcarbamoyl-substituted nitrones. methylcarbamoyl-substituted nitrones 282-318 heme oxygenase 2 Homo sapiens 12-15 17522121-17 2007 Increased HO-1 and HO-2 protein expression may increase the production of the antioxidants biliverdin and bilirubin, which are products of heme metabolism. Biliverdine 91-101 heme oxygenase 2 Homo sapiens 19-23 17687481-0 2007 Kinetics and branching ratio studies of the reaction of C2H5O2 + HO2 using chemical ionisation mass spectrometry. c2h5o2 56-62 heme oxygenase 2 Homo sapiens 65-68 17718462-0 2007 HNO3 forming channel of the HO2 + NO reaction as a function of pressure and temperature in the ranges of 72-600 Torr and 223-323 K. A high-pressure turbulent flow reactor coupled with a chemical ionization mass-spectrometer was used to determine the branching ratio of the HO(2) + NO reaction: HO(2) + NO --> OH + NO(2) (1a), HO(2) + NO --> HNO(3) (1b). oh + no 312-319 heme oxygenase 2 Homo sapiens 28-31 17718462-0 2007 HNO3 forming channel of the HO2 + NO reaction as a function of pressure and temperature in the ranges of 72-600 Torr and 223-323 K. A high-pressure turbulent flow reactor coupled with a chemical ionization mass-spectrometer was used to determine the branching ratio of the HO(2) + NO reaction: HO(2) + NO --> OH + NO(2) (1a), HO(2) + NO --> HNO(3) (1b). nitroxyl 0-3 heme oxygenase 2 Homo sapiens 28-31 17655283-3 2007 The total rate coefficient, k3, for the reaction HO2 + ClO --> products has been determined over the temperature range of 220-336 K at a total pressure of approximately 1.5 Torr of helium using the discharge-flow resonance-fluorescence technique. Helium 184-190 heme oxygenase 2 Homo sapiens 49-52 17655283-5 2007 HO2 molecules were formed by using either the termolecular association of H atoms in an excess of O2 or via the reaction of F atoms with an excess of H(2)O(2). Water 150-155 heme oxygenase 2 Homo sapiens 0-3 17522121-17 2007 Increased HO-1 and HO-2 protein expression may increase the production of the antioxidants biliverdin and bilirubin, which are products of heme metabolism. Bilirubin 106-115 heme oxygenase 2 Homo sapiens 19-23 17388354-0 2007 Kinetics and rate constants of the reaction CH2OH+O2-->CH2O+HO2 in the temperature range of 236-600 K. The kinetics and absolute rate constants of the gas-phase reaction of the hydroxymethyl radical (CH2OH) with molecular oxygen have been studied using laser photolysis/near-IR absorption spectroscopy. Formaldehyde 44-48 heme oxygenase 2 Homo sapiens 63-66 17388354-0 2007 Kinetics and rate constants of the reaction CH2OH+O2-->CH2O+HO2 in the temperature range of 236-600 K. The kinetics and absolute rate constants of the gas-phase reaction of the hydroxymethyl radical (CH2OH) with molecular oxygen have been studied using laser photolysis/near-IR absorption spectroscopy. Hydroxymethyl radical 180-201 heme oxygenase 2 Homo sapiens 63-66 17388354-0 2007 Kinetics and rate constants of the reaction CH2OH+O2-->CH2O+HO2 in the temperature range of 236-600 K. The kinetics and absolute rate constants of the gas-phase reaction of the hydroxymethyl radical (CH2OH) with molecular oxygen have been studied using laser photolysis/near-IR absorption spectroscopy. Hydroxymethyl radical 44-49 heme oxygenase 2 Homo sapiens 63-66 17388354-0 2007 Kinetics and rate constants of the reaction CH2OH+O2-->CH2O+HO2 in the temperature range of 236-600 K. The kinetics and absolute rate constants of the gas-phase reaction of the hydroxymethyl radical (CH2OH) with molecular oxygen have been studied using laser photolysis/near-IR absorption spectroscopy. Oxygen 225-231 heme oxygenase 2 Homo sapiens 63-66 17388354-1 2007 The reaction was tracked by monitoring the time-dependent changes in the production of the hydroperoxy radical (HO2) concentration. perhydroxyl radical 91-110 heme oxygenase 2 Homo sapiens 112-115 17455918-6 2007 The HO2 yield increases gradually until 500 K and sharply up to 40% over 500 K. The CH3OCH2O2 profile has a prompt rise, followed by a gradual decay whose time constant is consistent with slow HO2 formation. ch3och2o2 84-93 heme oxygenase 2 Homo sapiens 4-7 17566136-2 2007 The reaction is a complex process that involves, in the first stage, a pre-reactive hydrogen-bonded complex (C1), which is formed previous to two transition states (TS1 and TS2) involving the addition of the hydroxyl radical to ozone, and leads to the formation of HO4 polyoxide radical before the release of the products HO2 and O2. Hydrogen 84-92 heme oxygenase 2 Homo sapiens 322-325 17566136-2 2007 The reaction is a complex process that involves, in the first stage, a pre-reactive hydrogen-bonded complex (C1), which is formed previous to two transition states (TS1 and TS2) involving the addition of the hydroxyl radical to ozone, and leads to the formation of HO4 polyoxide radical before the release of the products HO2 and O2. Hydroxyl Radical 208-224 heme oxygenase 2 Homo sapiens 322-325 17566136-2 2007 The reaction is a complex process that involves, in the first stage, a pre-reactive hydrogen-bonded complex (C1), which is formed previous to two transition states (TS1 and TS2) involving the addition of the hydroxyl radical to ozone, and leads to the formation of HO4 polyoxide radical before the release of the products HO2 and O2. ho4 polyoxide radical 265-286 heme oxygenase 2 Homo sapiens 322-325 17388266-5 2007 The direct elimination of cyclohexene and HO2 from RO2 is included in the treatment using a modified rate constant of Cavallotti et al. ro2 51-54 heme oxygenase 2 Homo sapiens 42-45 17388389-1 2007 The kinetics of the reaction CO + HO2* --> CO2 + *OH was studied using a combination of ab initio electronic structure theory, transition state theory, and master equation modeling. Bicarbonates 46-55 heme oxygenase 2 Homo sapiens 34-37 17388389-3 2007 The classical energy barriers were found to be about 18 and 19 kcal/mol for CO + HO2* addition following the trans and cis paths, respectively. co + 76-80 heme oxygenase 2 Homo sapiens 81-84 17508833-0 2007 Formation of HO2 radicals from the photodissociation of H2O2 at 248 nm. Hydrogen Peroxide 56-60 heme oxygenase 2 Homo sapiens 13-16 17540772-3 2007 Unlike HO-1, HO-2 contains heme regulatory motifs (HRMs) (McCoubrey, W. K., Jr., Huang, T. J., and Maines, M. D. (1997) J. Biol. Heme 27-31 heme oxygenase 2 Homo sapiens 13-17 17540772-7 2007 Oxidized HO-2, which contains an intramolecular disulfide bond linking Cys(265) of HRM1 and Cys(282) of HRM2, binds heme tightly. Disulfides 48-57 heme oxygenase 2 Homo sapiens 9-13 17540772-7 2007 Oxidized HO-2, which contains an intramolecular disulfide bond linking Cys(265) of HRM1 and Cys(282) of HRM2, binds heme tightly. Cysteine 71-74 heme oxygenase 2 Homo sapiens 9-13 17540772-7 2007 Oxidized HO-2, which contains an intramolecular disulfide bond linking Cys(265) of HRM1 and Cys(282) of HRM2, binds heme tightly. Cysteine 92-95 heme oxygenase 2 Homo sapiens 9-13 17540772-7 2007 Oxidized HO-2, which contains an intramolecular disulfide bond linking Cys(265) of HRM1 and Cys(282) of HRM2, binds heme tightly. Heme 116-120 heme oxygenase 2 Homo sapiens 9-13 17540772-10 2007 Because HO-2 plays a key role in CO generation and heme homeostasis, reduction of the disulfide bond would be expected to increase intracellular free heme and decrease CO concentrations. Heme 51-55 heme oxygenase 2 Homo sapiens 8-12 17540772-10 2007 Because HO-2 plays a key role in CO generation and heme homeostasis, reduction of the disulfide bond would be expected to increase intracellular free heme and decrease CO concentrations. Disulfides 86-95 heme oxygenase 2 Homo sapiens 8-12 17540772-10 2007 Because HO-2 plays a key role in CO generation and heme homeostasis, reduction of the disulfide bond would be expected to increase intracellular free heme and decrease CO concentrations. Heme 150-154 heme oxygenase 2 Homo sapiens 8-12 17540772-11 2007 Thus, we propose that the HRMs in HO-2 constitute a thiol/disulfide redox switch that regulates the myriad physiological functions of HO-2, including its involvement in the hypoxic response in the carotid body, which involves interactions with a Ca(2+)-activated potassium channel. Sulfhydryl Compounds 52-57 heme oxygenase 2 Homo sapiens 34-38 17540772-11 2007 Thus, we propose that the HRMs in HO-2 constitute a thiol/disulfide redox switch that regulates the myriad physiological functions of HO-2, including its involvement in the hypoxic response in the carotid body, which involves interactions with a Ca(2+)-activated potassium channel. Sulfhydryl Compounds 52-57 heme oxygenase 2 Homo sapiens 134-138 17540772-11 2007 Thus, we propose that the HRMs in HO-2 constitute a thiol/disulfide redox switch that regulates the myriad physiological functions of HO-2, including its involvement in the hypoxic response in the carotid body, which involves interactions with a Ca(2+)-activated potassium channel. Disulfides 58-67 heme oxygenase 2 Homo sapiens 34-38 17540772-11 2007 Thus, we propose that the HRMs in HO-2 constitute a thiol/disulfide redox switch that regulates the myriad physiological functions of HO-2, including its involvement in the hypoxic response in the carotid body, which involves interactions with a Ca(2+)-activated potassium channel. Disulfides 58-67 heme oxygenase 2 Homo sapiens 134-138 17455918-0 2007 Analysis of HO2 and OH formation mechanisms using FM and UV spectroscopy in dimethyl ether oxidation. dimethyl ether 76-90 heme oxygenase 2 Homo sapiens 12-15 17455918-1 2007 Product formation pathways in the photolytically initiated oxidation of CH3OCH3 have been investigated as a function of temperature (298-600 K) and pressure (20-90 Torr) through the detection of HO2 and OH using Near-infrared frequency modulation spectroscopy, as well as the detection of CH3OCH2O2 using UV absorption spectroscopy. dimethyl ether 72-79 heme oxygenase 2 Homo sapiens 195-198 17455918-3 2007 The HO2 and OH yield is obtained by comparison with an established reference mixture, including CH3OH. Methanol 96-101 heme oxygenase 2 Homo sapiens 4-7 17455918-4 2007 The CH3OCH2O2 yield is also obtained through the procedure of estimating the CH3OCH2O2/HO2 ratio from their UV absorption. ch3och2o2 4-13 heme oxygenase 2 Homo sapiens 87-90 17455918-6 2007 The HO2 yield increases gradually until 500 K and sharply up to 40% over 500 K. The CH3OCH2O2 profile has a prompt rise, followed by a gradual decay whose time constant is consistent with slow HO2 formation. ch3och2o2 84-93 heme oxygenase 2 Homo sapiens 193-196 17455918-9 2007 We have also proposed that a new HCO formation pathway via QOOH isomerization to HOQO species and OH + CH3OCH2O2 --> HO2 + CH3OCH2O are to be considered, to account for the fast and slow HO2 formations, as well as the total yield. 7 alpha-hydroxy-4-cholesten-3-one 33-36 heme oxygenase 2 Homo sapiens 120-123 17455918-9 2007 We have also proposed that a new HCO formation pathway via QOOH isomerization to HOQO species and OH + CH3OCH2O2 --> HO2 + CH3OCH2O are to be considered, to account for the fast and slow HO2 formations, as well as the total yield. 7 alpha-hydroxy-4-cholesten-3-one 33-36 heme oxygenase 2 Homo sapiens 190-193 17455918-9 2007 We have also proposed that a new HCO formation pathway via QOOH isomerization to HOQO species and OH + CH3OCH2O2 --> HO2 + CH3OCH2O are to be considered, to account for the fast and slow HO2 formations, as well as the total yield. oh + ch3och2o2 98-112 heme oxygenase 2 Homo sapiens 120-123 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. 7 alpha-hydroxy-4-cholesten-3-one 73-76 heme oxygenase 2 Homo sapiens 25-28 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. 7 alpha-hydroxy-4-cholesten-3-one 73-76 heme oxygenase 2 Homo sapiens 439-442 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. Oxygen 26-28 heme oxygenase 2 Homo sapiens 439-442 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. 7 alpha-hydroxy-4-cholesten-3-one 126-129 heme oxygenase 2 Homo sapiens 25-28 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. ch3och2o2 200-209 heme oxygenase 2 Homo sapiens 25-28 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. oh + ch3och2o2 228-242 heme oxygenase 2 Homo sapiens 25-28 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. Methyl radical, methoxy- 200-207 heme oxygenase 2 Homo sapiens 25-28 17455918-11 2007 It was revealed that the HO2 formation mechanism changes at 500 K, i.e., HCO + O2 via HCHO + OH and the above proposed direct HCO formation dominates over 500 K, while a series of reactions following CH3OCH2O2 self-reaction and OH + CH3OCH2O2 reaction mainly contribute below 500 K. The pressure dependent rate constant of the CH3OCH2 thermal decomposition reaction has been separately measured since it has large negative sensitivity for HO2 formation and is essential to eliminate the ambiguity in the CH3OCH2 + O2 mechanism at higher temperature. ch3och2 + o2 504-516 heme oxygenase 2 Homo sapiens 25-28 17362045-9 2007 In fact, even some slight inhibition can be observed, due to the formation of chain-terminating HO2* radicals in the alcohol co-oxidation. Alcohols 117-124 heme oxygenase 2 Homo sapiens 96-99 17339115-3 2007 The imidazole-dioxolanes were all selective for the HO-1 isozyme (inducible) and exhibited substantially lower activity toward the HO-2 isozyme (constitutive). imidazole-dioxolanes 4-24 heme oxygenase 2 Homo sapiens 131-135 17131376-1 2007 The contribution of heme oxygenase HO-2, the primary source of bilirubin and carbon monoxide (CO) under physiological conditions, to the regulation of vascular function has remained largely unexplored. Bilirubin 63-72 heme oxygenase 2 Homo sapiens 35-39 17408452-8 2007 HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide. Biliverdine 130-140 heme oxygenase 2 Homo sapiens 33-37 17408452-8 2007 HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide. Iron 142-146 heme oxygenase 2 Homo sapiens 33-37 17408452-8 2007 HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide. Carbon Monoxide 152-167 heme oxygenase 2 Homo sapiens 33-37 17131376-3 2007 In vivo HO-2 siRNA treatment decreased the basal levels of EC-SOD, pAKT proteins (serine-473 and threonine-308), without changing Akt protein expression. Threonine 97-106 heme oxygenase 2 Homo sapiens 8-12 17131376-1 2007 The contribution of heme oxygenase HO-2, the primary source of bilirubin and carbon monoxide (CO) under physiological conditions, to the regulation of vascular function has remained largely unexplored. Carbon Monoxide 77-92 heme oxygenase 2 Homo sapiens 35-39 17131376-4 2007 HO-2 siRNA treatment increased 3-nitrotyrosine (3-NT) and apoptotic signaling kinase-1 (ASK-1) (P < 0.01). 3-nitrotyrosine 31-46 heme oxygenase 2 Homo sapiens 0-4 17131376-1 2007 The contribution of heme oxygenase HO-2, the primary source of bilirubin and carbon monoxide (CO) under physiological conditions, to the regulation of vascular function has remained largely unexplored. Carbon Monoxide 94-96 heme oxygenase 2 Homo sapiens 35-39 17131376-4 2007 HO-2 siRNA treatment increased 3-nitrotyrosine (3-NT) and apoptotic signaling kinase-1 (ASK-1) (P < 0.01). 3-nitrotyrosine 48-52 heme oxygenase 2 Homo sapiens 0-4 17131376-3 2007 In vivo HO-2 siRNA treatment decreased the basal levels of EC-SOD, pAKT proteins (serine-473 and threonine-308), without changing Akt protein expression. Serine 82-88 heme oxygenase 2 Homo sapiens 8-12 17674820-3 2007 It has been demonstrated that electrons with this energy can dissociate water and oxygen molecules and produce various reactive radicals (*OH, H*, O*, HO2*), molecular species (H2O2, H2, O2), ultraviolet radiation and shock waves. Water 72-77 heme oxygenase 2 Homo sapiens 151-154 17201391-0 2007 Reaction of O2 with the hydrogen atom in water up to 350 degrees C. The reaction of the H* atom with O2, giving the hydroperoxyl HO2* radical, has been investigated in pressurized water up to 350 degrees C using pulse radiolysis and deep-UV transient absorption spectroscopy. Hydrogen 24-32 heme oxygenase 2 Homo sapiens 129-132 17201391-0 2007 Reaction of O2 with the hydrogen atom in water up to 350 degrees C. The reaction of the H* atom with O2, giving the hydroperoxyl HO2* radical, has been investigated in pressurized water up to 350 degrees C using pulse radiolysis and deep-UV transient absorption spectroscopy. Water 41-46 heme oxygenase 2 Homo sapiens 129-132 17201391-0 2007 Reaction of O2 with the hydrogen atom in water up to 350 degrees C. The reaction of the H* atom with O2, giving the hydroperoxyl HO2* radical, has been investigated in pressurized water up to 350 degrees C using pulse radiolysis and deep-UV transient absorption spectroscopy. Oxygen 101-103 heme oxygenase 2 Homo sapiens 129-132 17305496-6 2007 Application of cGMP-activated phosphodiesterase-2 inhibitor EHNA did not prevent CO action, whereas inhibition of cGMP-inhibited phosphodiesterase-3 by quazinone has partially blocked the effect of CO. Utilizing immuno-histochemical methods CO-producing enzyme heme-oxygenase-2 (HO-2) was shown to be expressed in skeletal muscle fibers, mostly in sub-sarcolemmal region, karyolemma and sarcoplasmic reticulum. Cyclic GMP 114-118 heme oxygenase 2 Homo sapiens 261-277 17305496-6 2007 Application of cGMP-activated phosphodiesterase-2 inhibitor EHNA did not prevent CO action, whereas inhibition of cGMP-inhibited phosphodiesterase-3 by quazinone has partially blocked the effect of CO. Utilizing immuno-histochemical methods CO-producing enzyme heme-oxygenase-2 (HO-2) was shown to be expressed in skeletal muscle fibers, mostly in sub-sarcolemmal region, karyolemma and sarcoplasmic reticulum. Cyclic GMP 114-118 heme oxygenase 2 Homo sapiens 279-283 17305496-7 2007 Zn-protoporphirin-IX, the selective HO-2 blocker, has depressed Ach-release, suggesting the tonic activating effect of endogenous CO on pre-synaptic function. zn-protoporphirin-ix 0-20 heme oxygenase 2 Homo sapiens 36-40 17305496-7 2007 Zn-protoporphirin-IX, the selective HO-2 blocker, has depressed Ach-release, suggesting the tonic activating effect of endogenous CO on pre-synaptic function. Acetylcholine 64-67 heme oxygenase 2 Homo sapiens 36-40 17201391-0 2007 Reaction of O2 with the hydrogen atom in water up to 350 degrees C. The reaction of the H* atom with O2, giving the hydroperoxyl HO2* radical, has been investigated in pressurized water up to 350 degrees C using pulse radiolysis and deep-UV transient absorption spectroscopy. Oxygen 12-14 heme oxygenase 2 Homo sapiens 129-132 17674820-3 2007 It has been demonstrated that electrons with this energy can dissociate water and oxygen molecules and produce various reactive radicals (*OH, H*, O*, HO2*), molecular species (H2O2, H2, O2), ultraviolet radiation and shock waves. Oxygen 82-88 heme oxygenase 2 Homo sapiens 151-154 17112254-2 2006 The key step is found to be the abstraction of the hydrogen atom resulting in the formation of a PdI/HO2 (triplet) radical pair, which then proceeds to form a singlet palladium hydroperoxo species. Hydrogen 51-59 heme oxygenase 2 Homo sapiens 101-104 17181346-0 2006 Ionic association of hydroperoxide anion HO2- in the binding mean spherical approximation. hydroperoxide anion 21-40 heme oxygenase 2 Homo sapiens 41-44 17181346-4 2006 The band originates from an intramolecular electronic transition of the hydroperoxide anion HO2-, as indicated by the negligible temperature effect on the band position and confirmed by ab initio quantum mechanical calculations. hydroperoxide anion 72-91 heme oxygenase 2 Homo sapiens 92-95 17181346-5 2006 It is postulated that the bathochromic shift of the peroxide band that accompanies the increase in NaOH concentration originates from the formation of the ion pair (Na+HO2-). Peroxides 52-60 heme oxygenase 2 Homo sapiens 168-171 17181346-5 2006 It is postulated that the bathochromic shift of the peroxide band that accompanies the increase in NaOH concentration originates from the formation of the ion pair (Na+HO2-). Sodium Hydroxide 99-103 heme oxygenase 2 Homo sapiens 168-171 17064313-3 2006 Recent studies have identified HO-2 as a potential oxygen sensor. Oxygen 51-57 heme oxygenase 2 Homo sapiens 31-35 17064313-10 2006 Moreover, HO-2 knockdown caused heme accumulation in HeLa and HepG2 cells only when exposed to exogenous hemin. Heme 32-36 heme oxygenase 2 Homo sapiens 10-14 17064313-10 2006 Moreover, HO-2 knockdown caused heme accumulation in HeLa and HepG2 cells only when exposed to exogenous hemin. Hemin 105-110 heme oxygenase 2 Homo sapiens 10-14 17064313-11 2006 HO-2 knockdown may mimic a certain physiological change that is important in the maintenance of cellular heme homeostasis. Heme 105-109 heme oxygenase 2 Homo sapiens 0-4 16722671-7 2006 The combined rate constant from the present work and earlier work by Glaenzer and Troe (GT) is k(OH+NO2) = 2.25 x 10(-11) exp(-3831 K/T) cm3 molecule(-1) s(-1), which is a factor of 2 lower than the extrapolated direct value from Howard but agrees well with NO + HO2 --> OH + NO2 transformed with the updated equilibrium constants. oh+no2 97-103 heme oxygenase 2 Homo sapiens 263-266 16965065-1 2006 The hydroperoxyl radical (HO2) has long been considered as a prototype for statistical vibrational dynamics. Hydroperoxy radical 4-24 heme oxygenase 2 Homo sapiens 26-29 16740253-1 2006 Current concepts of cellular oxygen-sensing include an isoform of the neutrophil NADPH oxidase, different electron carrier units of the mitochondrial electron transport chain (ETC), heme oxygenase-2 (HO-2), and a subfamily of 2-oxoglutarate dependent dioxygenases termed HIF (hypoxia inducible factor) prolyl hydroxylases (PHDs) and HIF asparagyl hydroxylase FIH-1 (factor-inhibiting HIF). Oxygen 29-35 heme oxygenase 2 Homo sapiens 200-204 16787441-2 2006 Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide. Iron 152-156 heme oxygenase 2 Homo sapiens 87-103 16787441-2 2006 Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide. Carbon Monoxide 161-176 heme oxygenase 2 Homo sapiens 87-103 16787441-4 2006 Here we show that hypoxia (1% oxygen) reduces the expression levels of heme oxygenase-2 mRNA and protein after 48 h of incubation in human cell lines, including Jurkat T-lymphocytes, YN-1 and K562 erythroleukemia, HeLa cervical cancer, and HepG2 hepatoma, as judged by northern blot and western blot analyses. Oxygen 30-36 heme oxygenase 2 Homo sapiens 71-87 16789772-0 2006 Study of benzylperoxy radical using laser photolysis: ultraviolet spectrum, self-reaction, and reaction with HO2 kinetics. benzylperoxy radical 9-29 heme oxygenase 2 Homo sapiens 109-112 16722670-5 2006 The new thermochemistry of HO2, together with other arguments given in the present work, suggests that the previous equilibrium constant for NO + HO2 --> OH + NO2 was underestimated by a factor of approximately 2, implicating that the OH + NO2 rate was overestimated by the same factor. oh + no2 157-165 heme oxygenase 2 Homo sapiens 27-30 16722670-5 2006 The new thermochemistry of HO2, together with other arguments given in the present work, suggests that the previous equilibrium constant for NO + HO2 --> OH + NO2 was underestimated by a factor of approximately 2, implicating that the OH + NO2 rate was overestimated by the same factor. oh + no2 157-165 heme oxygenase 2 Homo sapiens 146-149 16722670-5 2006 The new thermochemistry of HO2, together with other arguments given in the present work, suggests that the previous equilibrium constant for NO + HO2 --> OH + NO2 was underestimated by a factor of approximately 2, implicating that the OH + NO2 rate was overestimated by the same factor. oh + no2 238-246 heme oxygenase 2 Homo sapiens 27-30 17047753-2 2006 All three oxygen species form very weak complexes with toluene and all also appear capable of abstracting a benzylic hydrogen atom to form the HO2 radical. Oxygen 10-16 heme oxygenase 2 Homo sapiens 143-146 17047753-2 2006 All three oxygen species form very weak complexes with toluene and all also appear capable of abstracting a benzylic hydrogen atom to form the HO2 radical. Hydrogen 117-125 heme oxygenase 2 Homo sapiens 143-146 16787441-2 2006 Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide. Biliverdine 140-150 heme oxygenase 2 Homo sapiens 87-103 16722670-5 2006 The new thermochemistry of HO2, together with other arguments given in the present work, suggests that the previous equilibrium constant for NO + HO2 --> OH + NO2 was underestimated by a factor of approximately 2, implicating that the OH + NO2 rate was overestimated by the same factor. oh + no2 238-246 heme oxygenase 2 Homo sapiens 146-149 16722671-7 2006 The combined rate constant from the present work and earlier work by Glaenzer and Troe (GT) is k(OH+NO2) = 2.25 x 10(-11) exp(-3831 K/T) cm3 molecule(-1) s(-1), which is a factor of 2 lower than the extrapolated direct value from Howard but agrees well with NO + HO2 --> OH + NO2 transformed with the updated equilibrium constants. oh + no2 274-282 heme oxygenase 2 Homo sapiens 263-266 16722671-0 2006 Reflected shock tube studies of high-temperature rate constants for OH + NO2 --> HO2 + NO and OH + HO2 --> H2O + O2. oh + no2 68-76 heme oxygenase 2 Homo sapiens 84-87 16722671-1 2006 The motivation for the present study comes from the preceding paper where it is suggested that accepted rate constants for OH + NO2 --> NO + HO2 are high by approximately 2. oh + no2 123-131 heme oxygenase 2 Homo sapiens 144-147 16722672-4 2006 According to the proposed kinetic scheme, the mutual sensitization of the oxidation of this natural gas blend and NO proceeds through the NO to NO2 conversion by HO2, CH3O2, and C2H5O2. Nitrogen Dioxide 144-147 heme oxygenase 2 Homo sapiens 162-165 16722672-6 2006 820 K) than at higher temperatures where the reaction of NO with HO2 controls the NO to NO2 conversion. Nitrogen Dioxide 88-91 heme oxygenase 2 Homo sapiens 65-68 16722672-8 2006 A simplified reaction scheme was delineated: NO + HO2 --> NO2 + OH followed by OH + CH4 --> CH3 + H2O and OH + C2H6 --> C2H5 + H2O. Nitrogen Dioxide 61-64 heme oxygenase 2 Homo sapiens 50-53 16722672-8 2006 A simplified reaction scheme was delineated: NO + HO2 --> NO2 + OH followed by OH + CH4 --> CH3 + H2O and OH + C2H6 --> C2H5 + H2O. Methane 87-90 heme oxygenase 2 Homo sapiens 50-53 16722672-8 2006 A simplified reaction scheme was delineated: NO + HO2 --> NO2 + OH followed by OH + CH4 --> CH3 + H2O and OH + C2H6 --> C2H5 + H2O. Ethyl radical 129-133 heme oxygenase 2 Homo sapiens 50-53 16722672-8 2006 A simplified reaction scheme was delineated: NO + HO2 --> NO2 + OH followed by OH + CH4 --> CH3 + H2O and OH + C2H6 --> C2H5 + H2O. Water 136-139 heme oxygenase 2 Homo sapiens 50-53 16722672-11 2006 The further reactions CH3O --> CH2O + H; CH2O + OH --> HCO + H2O; HCO + O2 --> HO2 + CO; and H + O2 + M --> HO2 + M complete the sequence. 7 alpha-hydroxy-4-cholesten-3-one 61-64 heme oxygenase 2 Homo sapiens 120-123 16722672-13 2006 The kinetic analyses indicate that in the NO-seeded conditions, the main production of OH proceeds via the same route, NO + HO2 --> NO2 + OH. Nitrogen Dioxide 135-138 heme oxygenase 2 Homo sapiens 124-127 16722699-4 2006 Other observed products were formaldehyde, CO2 and peroxy radicals HO2 and CH3C(O)O2. peroxy radicals 51-66 heme oxygenase 2 Homo sapiens 67-70 16722699-7 2006 The rate constant of the reaction CH3C(O)CHOH + O2 --> CH3C(O)CHO + HO2 at 298 K, (3.0 +/- 0.6) x 10(-12) cm3 molecule(-1) s(-1), was estimated by computer simulation of the concentration-time profiles of the CH3C(O)CHO product. choh 41-45 heme oxygenase 2 Homo sapiens 71-74 16722709-2 2006 On the microsecond time scale, [HO2] exhibited a time dependence consistent with a mechanism in which [HO2] approached equilibrium via HO2 + HO2.CH3OH (3, -3). Methanol 145-150 heme oxygenase 2 Homo sapiens 103-106 16722699-7 2006 The rate constant of the reaction CH3C(O)CHOH + O2 --> CH3C(O)CHO + HO2 at 298 K, (3.0 +/- 0.6) x 10(-12) cm3 molecule(-1) s(-1), was estimated by computer simulation of the concentration-time profiles of the CH3C(O)CHO product. Oxygen 48-50 heme oxygenase 2 Homo sapiens 71-74 16722709-2 2006 On the microsecond time scale, [HO2] exhibited a time dependence consistent with a mechanism in which [HO2] approached equilibrium via HO2 + HO2.CH3OH (3, -3). Methanol 145-150 heme oxygenase 2 Homo sapiens 103-106 16722709-4 2006 The effective bimolecular rate constant, k3, for formation of the HO2.CH3OH complex is .10(-15).exp[(1800 +/- 500)/T] cm3 molecule(-1) s(-1) at 100 Torr (1 sigma). Methanol 70-75 heme oxygenase 2 Homo sapiens 66-69 16722699-7 2006 The rate constant of the reaction CH3C(O)CHOH + O2 --> CH3C(O)CHO + HO2 at 298 K, (3.0 +/- 0.6) x 10(-12) cm3 molecule(-1) s(-1), was estimated by computer simulation of the concentration-time profiles of the CH3C(O)CHO product. CAV protocol 41-44 heme oxygenase 2 Homo sapiens 71-74 16722709-5 2006 Ab initio calculations of the optimized structure and energetics of the HO2.CH3OH complex were performed at the CCSD(T)/6-311++G(3df,3pd)//MP2(full)/6-311++G(2df,2pd) level. Methanol 76-81 heme oxygenase 2 Homo sapiens 72-75 16722699-7 2006 The rate constant of the reaction CH3C(O)CHOH + O2 --> CH3C(O)CHO + HO2 at 298 K, (3.0 +/- 0.6) x 10(-12) cm3 molecule(-1) s(-1), was estimated by computer simulation of the concentration-time profiles of the CH3C(O)CHO product. CAV protocol 65-68 heme oxygenase 2 Homo sapiens 71-74 16722709-6 2006 The complex was found to have a strong hydrogen bond (D(e) = 43.9 kJ mol(-1)) with the hydrogen in HO2 binding to the oxygen in CH3OH. Hydrogen 39-47 heme oxygenase 2 Homo sapiens 99-102 16722709-6 2006 The complex was found to have a strong hydrogen bond (D(e) = 43.9 kJ mol(-1)) with the hydrogen in HO2 binding to the oxygen in CH3OH. Hydrogen 87-95 heme oxygenase 2 Homo sapiens 99-102 16722705-8 2006 Of these two parameter sets, one is far more consistent with recent observations of trans-HOONO decay, isotopic scrambling, and HONO2 production from HO2 + NO. Nitric Acid 128-133 heme oxygenase 2 Homo sapiens 150-153 16722709-6 2006 The complex was found to have a strong hydrogen bond (D(e) = 43.9 kJ mol(-1)) with the hydrogen in HO2 binding to the oxygen in CH3OH. Oxygen 118-124 heme oxygenase 2 Homo sapiens 99-102 16722705-11 2006 This has significant implications for observed HOONO behavior and also HONO2 formation in the atmosphere from both HO2 + NO and OH + NO2. Nitric Acid 71-76 heme oxygenase 2 Homo sapiens 115-118 16722709-6 2006 The complex was found to have a strong hydrogen bond (D(e) = 43.9 kJ mol(-1)) with the hydrogen in HO2 binding to the oxygen in CH3OH. Methanol 128-133 heme oxygenase 2 Homo sapiens 99-102 16722709-0 2006 Experimental and ab initio study of the HO2.CH3OH complex: thermodynamics and kinetics of formation. Methanol 44-49 heme oxygenase 2 Homo sapiens 40-43 16722709-1 2006 Near-infrared spectroscopy was used to monitor HO2 formed by pulsed laser photolysis of Cl2-O2-CH3OH-N2 mixtures. cl2-o2 88-94 heme oxygenase 2 Homo sapiens 47-50 16722709-1 2006 Near-infrared spectroscopy was used to monitor HO2 formed by pulsed laser photolysis of Cl2-O2-CH3OH-N2 mixtures. Methanol 95-100 heme oxygenase 2 Homo sapiens 47-50 16722709-1 2006 Near-infrared spectroscopy was used to monitor HO2 formed by pulsed laser photolysis of Cl2-O2-CH3OH-N2 mixtures. Nitrogen 101-103 heme oxygenase 2 Homo sapiens 47-50 16722709-2 2006 On the microsecond time scale, [HO2] exhibited a time dependence consistent with a mechanism in which [HO2] approached equilibrium via HO2 + HO2.CH3OH (3, -3). Methanol 145-150 heme oxygenase 2 Homo sapiens 32-35 16722709-2 2006 On the microsecond time scale, [HO2] exhibited a time dependence consistent with a mechanism in which [HO2] approached equilibrium via HO2 + HO2.CH3OH (3, -3). Methanol 145-150 heme oxygenase 2 Homo sapiens 103-106 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Heme 4-8 heme oxygenase 2 Homo sapiens 81-85 16627294-3 2006 In the last half-century, the chemical mechanisms operating within the ozone layer have been shown to include very efficient catalytic chain reactions involving the chemical species HO, HO2, NO, NO2, Cl and ClO. clo 207-210 heme oxygenase 2 Homo sapiens 186-189 16620108-0 2006 Role of interstitial voids in oxides on formation and stabilization of reactive radicals: interstitial HO2 radicals in F2-laser-irradiated amorphous SiO2. Silicon Dioxide 149-153 heme oxygenase 2 Homo sapiens 103-106 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Iron 262-266 heme oxygenase 2 Homo sapiens 81-85 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Carbon Monoxide 271-286 heme oxygenase 2 Homo sapiens 81-85 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Carbon Monoxide 288-290 heme oxygenase 2 Homo sapiens 81-85 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Biliverdine 184-194 heme oxygenase 2 Homo sapiens 81-85 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Bilirubin 199-208 heme oxygenase 2 Homo sapiens 81-85 16526652-0 2006 Exploration of the potential energy surfaces, prediction of atmospheric concentrations, and prediction of vibrational spectra for the HO2...(H2O)n (n = 1-2) hydrogen bonded complexes. Hydrogen 157-165 heme oxygenase 2 Homo sapiens 134-137 16539423-2 2006 This reaction involves the formation of H2CO + HO2 radical in a process that is computed to be exothermic by 57 kcal/mol. Formaldehyde 40-44 heme oxygenase 2 Homo sapiens 47-50 16526652-1 2006 The hydroperoxy radical (HO2) plays a critical role in Earth"s atmospheric chemistry as a component of many important reactions. perhydroxyl radical 4-23 heme oxygenase 2 Homo sapiens 25-28 16526652-4 2006 We predict that when the HO2 concentration is on the order of 10(8) molecules x cm(-3) at 298 K, that the number of HO2...H2O complexes is on the order of 10(7) molecules x cm(-3) and the number of HO2...(H2O)2 complexes is on the order of 10(6) molecules x cm(-3). Water 122-125 heme oxygenase 2 Homo sapiens 25-28 16526652-0 2006 Exploration of the potential energy surfaces, prediction of atmospheric concentrations, and prediction of vibrational spectra for the HO2...(H2O)n (n = 1-2) hydrogen bonded complexes. Water 141-144 heme oxygenase 2 Homo sapiens 134-137 16526652-4 2006 We predict that when the HO2 concentration is on the order of 10(8) molecules x cm(-3) at 298 K, that the number of HO2...H2O complexes is on the order of 10(7) molecules x cm(-3) and the number of HO2...(H2O)2 complexes is on the order of 10(6) molecules x cm(-3). Water 122-125 heme oxygenase 2 Homo sapiens 116-119 16526652-4 2006 We predict that when the HO2 concentration is on the order of 10(8) molecules x cm(-3) at 298 K, that the number of HO2...H2O complexes is on the order of 10(7) molecules x cm(-3) and the number of HO2...(H2O)2 complexes is on the order of 10(6) molecules x cm(-3). Water 122-125 heme oxygenase 2 Homo sapiens 116-119 16526652-4 2006 We predict that when the HO2 concentration is on the order of 10(8) molecules x cm(-3) at 298 K, that the number of HO2...H2O complexes is on the order of 10(7) molecules x cm(-3) and the number of HO2...(H2O)2 complexes is on the order of 10(6) molecules x cm(-3). Water 205-208 heme oxygenase 2 Homo sapiens 25-28 16526652-4 2006 We predict that when the HO2 concentration is on the order of 10(8) molecules x cm(-3) at 298 K, that the number of HO2...H2O complexes is on the order of 10(7) molecules x cm(-3) and the number of HO2...(H2O)2 complexes is on the order of 10(6) molecules x cm(-3). Water 205-208 heme oxygenase 2 Homo sapiens 116-119 16526652-4 2006 We predict that when the HO2 concentration is on the order of 10(8) molecules x cm(-3) at 298 K, that the number of HO2...H2O complexes is on the order of 10(7) molecules x cm(-3) and the number of HO2...(H2O)2 complexes is on the order of 10(6) molecules x cm(-3). Water 205-208 heme oxygenase 2 Homo sapiens 116-119 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 38-41 heme oxygenase 2 Homo sapiens 32-35 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 38-41 heme oxygenase 2 Homo sapiens 104-107 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 38-41 heme oxygenase 2 Homo sapiens 104-107 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 38-41 heme oxygenase 2 Homo sapiens 104-107 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 38-41 heme oxygenase 2 Homo sapiens 104-107 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 110-113 heme oxygenase 2 Homo sapiens 32-35 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 110-113 heme oxygenase 2 Homo sapiens 104-107 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 110-113 heme oxygenase 2 Homo sapiens 104-107 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 110-113 heme oxygenase 2 Homo sapiens 104-107 16526652-5 2006 Using the computed abundance of HO2...H2O, we predict that, at 298 K, the bimolecular rate constant for HO2...H2O + HO2 is about 10 times that for HO2 + HO2. Water 110-113 heme oxygenase 2 Homo sapiens 104-107 16435814-0 2006 Quantum mechanical rate constants for H + O2 <--> O + OH and H + O2 --> HO2 reactions. Oxygen 42-44 heme oxygenase 2 Homo sapiens 81-84 16467393-3 2006 It is produced from heme by a constitutively expressed enzyme [heme oxygenase (HO)-2] expressed highly in the brain and by an inducible enzyme (HO-1). Heme 20-24 heme oxygenase 2 Homo sapiens 63-84 16513981-0 2006 The rotational spectrum of the water-hydroperoxy radical (H2O-HO2) complex. Water 31-36 heme oxygenase 2 Homo sapiens 62-65 16513981-0 2006 The rotational spectrum of the water-hydroperoxy radical (H2O-HO2) complex. perhydroxyl radical 37-56 heme oxygenase 2 Homo sapiens 62-65 16513981-2 2006 We observed pure rotational transitions of the water-hydroperoxy radical complex, H2O-HO2, in a supersonic jet by means of a Fourier transform microwave spectrometer combined with a double-resonance technique. Water 47-52 heme oxygenase 2 Homo sapiens 86-89 16513981-2 2006 We observed pure rotational transitions of the water-hydroperoxy radical complex, H2O-HO2, in a supersonic jet by means of a Fourier transform microwave spectrometer combined with a double-resonance technique. perhydroxyl radical 53-72 heme oxygenase 2 Homo sapiens 86-89 16513981-2 2006 We observed pure rotational transitions of the water-hydroperoxy radical complex, H2O-HO2, in a supersonic jet by means of a Fourier transform microwave spectrometer combined with a double-resonance technique. Water 82-85 heme oxygenase 2 Homo sapiens 86-89 16435814-0 2006 Quantum mechanical rate constants for H + O2 <--> O + OH and H + O2 --> HO2 reactions. perhydroxyl radical 38-44 heme oxygenase 2 Homo sapiens 81-84 16471577-4 2006 Stronger acids result in protonation of the superoxide followed by reduction to produce HO2-. stronger 0-8 heme oxygenase 2 Homo sapiens 88-91 16683710-0 2006 In search of the acute oxygen sensor: functional proteomics and acute regulation of large-conductance, calcium-activated potassium channels by hemeoxygenase-2. Oxygen 23-29 heme oxygenase 2 Homo sapiens 143-158 16471577-4 2006 Stronger acids result in protonation of the superoxide followed by reduction to produce HO2-. Superoxides 44-54 heme oxygenase 2 Homo sapiens 88-91 16471577-7 2006 The reaction occurring at the second peak is a concerted proton and electron transfer (CPET) in which the electron is transferred to superoxide and a proton is transferred from HA to the superoxide, forming HO2- and A- in a concerted process. Superoxides 133-143 heme oxygenase 2 Homo sapiens 207-210 16471577-7 2006 The reaction occurring at the second peak is a concerted proton and electron transfer (CPET) in which the electron is transferred to superoxide and a proton is transferred from HA to the superoxide, forming HO2- and A- in a concerted process. histidinoalanine 177-179 heme oxygenase 2 Homo sapiens 207-210 16471577-7 2006 The reaction occurring at the second peak is a concerted proton and electron transfer (CPET) in which the electron is transferred to superoxide and a proton is transferred from HA to the superoxide, forming HO2- and A- in a concerted process. Superoxides 187-197 heme oxygenase 2 Homo sapiens 207-210 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Formaldehyde 82-86 heme oxygenase 2 Homo sapiens 217-220 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. CAV protocol 100-103 heme oxygenase 2 Homo sapiens 89-92 16366658-0 2005 Direct dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2. Hydrogen 29-37 heme oxygenase 2 Homo sapiens 66-69 16366658-0 2005 Direct dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2. Formaldehyde 59-63 heme oxygenase 2 Homo sapiens 66-69 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Formaldehyde 82-86 heme oxygenase 2 Homo sapiens 89-92 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. CAV protocol 100-103 heme oxygenase 2 Homo sapiens 217-220 16366658-0 2005 Direct dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2. CAV protocol 77-80 heme oxygenase 2 Homo sapiens 66-69 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Hydrogen Peroxide 106-110 heme oxygenase 2 Homo sapiens 89-92 16366658-0 2005 Direct dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2. Hydrogen Peroxide 83-87 heme oxygenase 2 Homo sapiens 66-69 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Hydrogen Peroxide 106-110 heme oxygenase 2 Homo sapiens 217-220 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Hydrogen 52-60 heme oxygenase 2 Homo sapiens 89-92 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Hydrogen 52-60 heme oxygenase 2 Homo sapiens 217-220 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Formaldehyde 232-236 heme oxygenase 2 Homo sapiens 89-92 16366658-1 2005 We present a direct ab initio dynamics study on the hydrogen abstraction reaction CH2O + HO2 --> CHO + H2O2, which is predicted to have four possible reaction channels caused by different attacking orientations of HO2 radical to CH2O. Formaldehyde 232-236 heme oxygenase 2 Homo sapiens 217-220 16137652-0 2005 Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction. Oxygen 22-24 heme oxygenase 2 Homo sapiens 0-15 16382109-3 2005 Inducible HO (HO-1) and constitutive HO (HO-2) are mostly recognized for their roles in the oxidation of heme and production of CO and biliverdin, whereas the biological function of the third HO isoform, HO-3, is still unclear. Heme 105-109 heme oxygenase 2 Homo sapiens 41-45 16382109-3 2005 Inducible HO (HO-1) and constitutive HO (HO-2) are mostly recognized for their roles in the oxidation of heme and production of CO and biliverdin, whereas the biological function of the third HO isoform, HO-3, is still unclear. Carbon Monoxide 128-130 heme oxygenase 2 Homo sapiens 41-45 16382109-3 2005 Inducible HO (HO-1) and constitutive HO (HO-2) are mostly recognized for their roles in the oxidation of heme and production of CO and biliverdin, whereas the biological function of the third HO isoform, HO-3, is still unclear. Biliverdine 135-145 heme oxygenase 2 Homo sapiens 41-45 16043027-10 2005 These data indicate that when HO-2 cannot metabolize the prooxidant heme, more cytotoxicity is found, whereas, interestingly, the catalytically inactive HO-2H45A was also able to protect cells against oxidative stress injury. Heme 68-72 heme oxygenase 2 Homo sapiens 30-34 16833272-0 2005 A systematic computational study of the reactions of HO2 with RO2: the HO2 + CH2ClO2, CHCl2O2, and CCl3O2 reactions. ro2 62-65 heme oxygenase 2 Homo sapiens 53-56 16833272-0 2005 A systematic computational study of the reactions of HO2 with RO2: the HO2 + CH2ClO2, CHCl2O2, and CCl3O2 reactions. ro2 62-65 heme oxygenase 2 Homo sapiens 71-74 16833272-0 2005 A systematic computational study of the reactions of HO2 with RO2: the HO2 + CH2ClO2, CHCl2O2, and CCl3O2 reactions. ch2clo2 77-84 heme oxygenase 2 Homo sapiens 53-56 16833272-0 2005 A systematic computational study of the reactions of HO2 with RO2: the HO2 + CH2ClO2, CHCl2O2, and CCl3O2 reactions. ch2clo2 77-84 heme oxygenase 2 Homo sapiens 71-74 16833272-0 2005 A systematic computational study of the reactions of HO2 with RO2: the HO2 + CH2ClO2, CHCl2O2, and CCl3O2 reactions. chcl2o2 86-93 heme oxygenase 2 Homo sapiens 53-56 16833272-0 2005 A systematic computational study of the reactions of HO2 with RO2: the HO2 + CH2ClO2, CHCl2O2, and CCl3O2 reactions. Methyldioxy, trichloro- 99-105 heme oxygenase 2 Homo sapiens 53-56 15964921-7 2005 Although inhibition of nitric oxide synthase (NOS) with N(omega)-nitro-l-arginine (l-NNA) did not alter basal HO-2 catalytic activity or CO production, l-NNA blocked glutamate stimulation of HO-2 activity and CO production. Nitroarginine 152-157 heme oxygenase 2 Homo sapiens 191-195 15964921-8 2005 Furthermore, the NO donor sodium nitroprusside mimicked the actions of glutamate on HO-2 and CO production. Nitroprusside 26-46 heme oxygenase 2 Homo sapiens 84-88 15964921-8 2005 Furthermore, the NO donor sodium nitroprusside mimicked the actions of glutamate on HO-2 and CO production. Glutamic Acid 71-80 heme oxygenase 2 Homo sapiens 84-88 15964921-9 2005 The action of NO appears to be via cGMP because 8-bromo-cGMP mimics and 1H-[1,2,4]oxadiazole-[4,3-a]quinoxalin-1-one (ODQ) blocks glutamate stimulation of CO production and HO-2 catalytic activity. Cyclic GMP 35-39 heme oxygenase 2 Homo sapiens 173-177 15964921-9 2005 The action of NO appears to be via cGMP because 8-bromo-cGMP mimics and 1H-[1,2,4]oxadiazole-[4,3-a]quinoxalin-1-one (ODQ) blocks glutamate stimulation of CO production and HO-2 catalytic activity. 1h-[1,2,4]oxadiazole-[4,3-a]quinoxalin-1-one 72-116 heme oxygenase 2 Homo sapiens 173-177 15964921-11 2005 Conversely, inhibition of calmodulin with calmidazolium chloride blocked glutamate stimulation of CO production and reduced HO-2 catalytic activity. calmidazolium 42-64 heme oxygenase 2 Homo sapiens 124-128 15964921-12 2005 These data suggest that glutamate may activate NOS producing NO that leads to CO synthesis via a cGMP-dependent elevation of HO-2 catalytic activity. Glutamic Acid 24-33 heme oxygenase 2 Homo sapiens 125-129 15964921-12 2005 These data suggest that glutamate may activate NOS producing NO that leads to CO synthesis via a cGMP-dependent elevation of HO-2 catalytic activity. Cyclic GMP 97-101 heme oxygenase 2 Homo sapiens 125-129 16853105-3 2005 In alkaline solutions, a potential dependent band at 1268 cm(-1), which we assigned to the antisymmetric bending mode of OOH of adsorbed HO2-, was observed between 0.1 and -0.6 V versus Ag AgCl, Cl-, exactly in the potential range where the ORR occurred. OOH 121-124 heme oxygenase 2 Homo sapiens 137-140 16853105-3 2005 In alkaline solutions, a potential dependent band at 1268 cm(-1), which we assigned to the antisymmetric bending mode of OOH of adsorbed HO2-, was observed between 0.1 and -0.6 V versus Ag AgCl, Cl-, exactly in the potential range where the ORR occurred. silver chloride 189-193 heme oxygenase 2 Homo sapiens 137-140 16853105-7 2005 This finding may imply that the interaction between HO2- and Au surfaces is very weak in acidic solutions, in agreement with the observed 2e- reduction mechanism. Gold 61-63 heme oxygenase 2 Homo sapiens 52-55 16379285-2 2005 HO2 x CH3 OH (Thr = DL-Threonine, Phen = o-Phenanthroline), which has not been published, was synthesized and characterized by elemental analysis, IR spectroscopy, and TG-DTA. Threonine 14-17 heme oxygenase 2 Homo sapiens 0-3 16379285-2 2005 HO2 x CH3 OH (Thr = DL-Threonine, Phen = o-Phenanthroline), which has not been published, was synthesized and characterized by elemental analysis, IR spectroscopy, and TG-DTA. DL-Threonine 20-32 heme oxygenase 2 Homo sapiens 0-3 16379285-2 2005 HO2 x CH3 OH (Thr = DL-Threonine, Phen = o-Phenanthroline), which has not been published, was synthesized and characterized by elemental analysis, IR spectroscopy, and TG-DTA. 1,10-phenanthroline 34-38 heme oxygenase 2 Homo sapiens 0-3 16379285-2 2005 HO2 x CH3 OH (Thr = DL-Threonine, Phen = o-Phenanthroline), which has not been published, was synthesized and characterized by elemental analysis, IR spectroscopy, and TG-DTA. 1,10-phenanthroline 41-57 heme oxygenase 2 Homo sapiens 0-3 16379285-2 2005 HO2 x CH3 OH (Thr = DL-Threonine, Phen = o-Phenanthroline), which has not been published, was synthesized and characterized by elemental analysis, IR spectroscopy, and TG-DTA. Thioguanine 168-170 heme oxygenase 2 Homo sapiens 0-3 16379285-2 2005 HO2 x CH3 OH (Thr = DL-Threonine, Phen = o-Phenanthroline), which has not been published, was synthesized and characterized by elemental analysis, IR spectroscopy, and TG-DTA. deoxythymidylyl-3'-5'-deoxyadenylate 171-174 heme oxygenase 2 Homo sapiens 0-3 16358018-5 2005 However, formation of the H-transfer product CS + HO2 is kinetically much less feasible, i.e., the direct mechanism has barriers of 14.3 and 8.7 kcal mol(-1), whereas the indirect mechanism has barriers of 12.6 and 10.7 kcal mol(-1), respectively. Cesium 45-47 heme oxygenase 2 Homo sapiens 50-53 16834172-5 2005 Since CH2O is a major product in both reactions, reliable rates for the reaction CH2O + O2 --> HCO + HO2 could be derived from [OH]t and [O]t experiments over the T-range 1587-2109 K. The combined linear least-squares fit result, k = 1.34 x 10(-8) exp(-26883 K/T) cm3 molecule(-1) s(-1), and a recent VTST calculation clearly overlap within the uncertainties in both studies. Formaldehyde 6-10 heme oxygenase 2 Homo sapiens 104-107 16834172-5 2005 Since CH2O is a major product in both reactions, reliable rates for the reaction CH2O + O2 --> HCO + HO2 could be derived from [OH]t and [O]t experiments over the T-range 1587-2109 K. The combined linear least-squares fit result, k = 1.34 x 10(-8) exp(-26883 K/T) cm3 molecule(-1) s(-1), and a recent VTST calculation clearly overlap within the uncertainties in both studies. 7 alpha-hydroxy-4-cholesten-3-one 98-101 heme oxygenase 2 Homo sapiens 104-107 16834172-6 2005 Finally, a high sensitivity for the reaction OH + O2 --> HO2 + O was noted at high temperature in the O-atom data set simulations. oh + o2 -- 45-55 heme oxygenase 2 Homo sapiens 60-63 16833996-0 2005 Formation of nitric acid in the gas-phase HO2 + NO reaction: effects of temperature and water vapor. Nitric Acid 13-24 heme oxygenase 2 Homo sapiens 42-45 16833996-0 2005 Formation of nitric acid in the gas-phase HO2 + NO reaction: effects of temperature and water vapor. Water 88-93 heme oxygenase 2 Homo sapiens 42-45 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). Nitric Acid 149-160 heme oxygenase 2 Homo sapiens 175-178 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). Nitric Acid 149-160 heme oxygenase 2 Homo sapiens 242-245 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). Nitric Acid 149-160 heme oxygenase 2 Homo sapiens 242-245 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). Nitric Acid 162-166 heme oxygenase 2 Homo sapiens 175-178 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). Nitric Acid 162-166 heme oxygenase 2 Homo sapiens 242-245 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). Nitric Acid 162-166 heme oxygenase 2 Homo sapiens 242-245 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). oh + no2 258-266 heme oxygenase 2 Homo sapiens 175-178 16833996-1 2005 A high-pressure turbulent flow reactor coupled with a chemical ionization mass spectrometer was used to investigate the minor channel (1b) producing nitric acid, HNO3, in the HO2 + NO reaction for which only one channel (1a) is known so far: HO2 + NO --> OH + NO2 (1a), HO2 + NO --> HNO3 (1b). Nitric Acid 289-293 heme oxygenase 2 Homo sapiens 175-178 19791408-2 2005 The HO2 self-reaction rate coefficient (HO2 + HO2 --> H2O2 + O2 (R1)) has been determined as a function of temperature (236 < T < 309 K, at 760 Torr) and pressure (100 < p < 760 Torr, at 296 K). Hydrogen Peroxide 57-61 heme oxygenase 2 Homo sapiens 40-43 19791408-0 2005 Kinetics of the gas phase HO2 self-reaction: effects of temperature, pressure, water and methanol vapours. Water 79-84 heme oxygenase 2 Homo sapiens 26-29 16035836-7 2005 The quantum J-specific unimolecular dissociation rates for HO2-->H+O2 in the energy range from 2.114 to 2.596 eV have been reported for the first time, and comparisons with the results of Troe and co-workers [J. Chem. perhydroxyl radical 68-72 heme oxygenase 2 Homo sapiens 59-62 19791408-2 2005 The HO2 self-reaction rate coefficient (HO2 + HO2 --> H2O2 + O2 (R1)) has been determined as a function of temperature (236 < T < 309 K, at 760 Torr) and pressure (100 < p < 760 Torr, at 296 K). Hydrogen Peroxide 57-61 heme oxygenase 2 Homo sapiens 40-43 19791408-0 2005 Kinetics of the gas phase HO2 self-reaction: effects of temperature, pressure, water and methanol vapours. Methanol 89-97 heme oxygenase 2 Homo sapiens 26-29 15918699-6 2005 The determined structure is planar and almost T shaped, where the argon atom is slightly shifted to the hydrogen atom of HO2. Argon 66-71 heme oxygenase 2 Homo sapiens 121-124 19791408-1 2005 The kinetics of the gas phase HO2 self-reaction have been studied using flash photolysis of Cl2/CH3OH/O2/N2 mixtures coupled with time-resolved broadband UV absorption spectroscopy. Chlorine 92-95 heme oxygenase 2 Homo sapiens 30-33 19791408-1 2005 The kinetics of the gas phase HO2 self-reaction have been studied using flash photolysis of Cl2/CH3OH/O2/N2 mixtures coupled with time-resolved broadband UV absorption spectroscopy. Methanol 96-101 heme oxygenase 2 Homo sapiens 30-33 19791408-1 2005 The kinetics of the gas phase HO2 self-reaction have been studied using flash photolysis of Cl2/CH3OH/O2/N2 mixtures coupled with time-resolved broadband UV absorption spectroscopy. Nitrogen 105-107 heme oxygenase 2 Homo sapiens 30-33 19791408-2 2005 The HO2 self-reaction rate coefficient (HO2 + HO2 --> H2O2 + O2 (R1)) has been determined as a function of temperature (236 < T < 309 K, at 760 Torr) and pressure (100 < p < 760 Torr, at 296 K). Hydrogen Peroxide 57-61 heme oxygenase 2 Homo sapiens 4-7 16833760-1 2005 HO2*-initiated oxidation of ketones/aldehydes near the tropopause. Ketones 28-35 heme oxygenase 2 Homo sapiens 0-3 16833760-1 2005 HO2*-initiated oxidation of ketones/aldehydes near the tropopause. Aldehydes 36-45 heme oxygenase 2 Homo sapiens 0-3 16833760-5 2005 On the basis of the G2M//B3LYP-DFT PES, the kinetics of the approximately equal to 15 kcal/mol endothermal alpha-hydroxy-alkylperoxyl decompositions and of the reverse HO2*+ ketone/aldehyde reactions were evaluated using multiconformer transition state theory. Ketones 174-180 heme oxygenase 2 Homo sapiens 168-171 16833760-5 2005 On the basis of the G2M//B3LYP-DFT PES, the kinetics of the approximately equal to 15 kcal/mol endothermal alpha-hydroxy-alkylperoxyl decompositions and of the reverse HO2*+ ketone/aldehyde reactions were evaluated using multiconformer transition state theory. Aldehydes 181-189 heme oxygenase 2 Homo sapiens 168-171 16833760-7 2005 Contrary to current views, HO2* is found to react as fast with ketones as with aldehydes. Ketones 63-70 heme oxygenase 2 Homo sapiens 27-30 16833760-7 2005 Contrary to current views, HO2* is found to react as fast with ketones as with aldehydes. Aldehydes 79-88 heme oxygenase 2 Homo sapiens 27-30 16833760-11 2005 On the other hand, an RRKM-master equation analysis shows that hot alpha-hydroxy-alkylperoxyls formed by the addition of O(2) to C(1)-, C(2)-, and C(3)-alpha-hydroxy-alkyl radicals will quasi-uniquely fragment to HO2* plus the carbonyl under all atmospheric conditions. alpha-hydroxy-alkylperoxyls 67-94 heme oxygenase 2 Homo sapiens 213-216 16833760-11 2005 On the other hand, an RRKM-master equation analysis shows that hot alpha-hydroxy-alkylperoxyls formed by the addition of O(2) to C(1)-, C(2)-, and C(3)-alpha-hydroxy-alkyl radicals will quasi-uniquely fragment to HO2* plus the carbonyl under all atmospheric conditions. o(2) 121-125 heme oxygenase 2 Homo sapiens 213-216 16833760-11 2005 On the other hand, an RRKM-master equation analysis shows that hot alpha-hydroxy-alkylperoxyls formed by the addition of O(2) to C(1)-, C(2)-, and C(3)-alpha-hydroxy-alkyl radicals will quasi-uniquely fragment to HO2* plus the carbonyl under all atmospheric conditions. Carbon 129-130 heme oxygenase 2 Homo sapiens 213-216 16833760-11 2005 On the other hand, an RRKM-master equation analysis shows that hot alpha-hydroxy-alkylperoxyls formed by the addition of O(2) to C(1)-, C(2)-, and C(3)-alpha-hydroxy-alkyl radicals will quasi-uniquely fragment to HO2* plus the carbonyl under all atmospheric conditions. Carbon 136-137 heme oxygenase 2 Homo sapiens 213-216 16833760-11 2005 On the other hand, an RRKM-master equation analysis shows that hot alpha-hydroxy-alkylperoxyls formed by the addition of O(2) to C(1)-, C(2)-, and C(3)-alpha-hydroxy-alkyl radicals will quasi-uniquely fragment to HO2* plus the carbonyl under all atmospheric conditions. c(3)-alpha-hydroxy-alkyl radicals 147-180 heme oxygenase 2 Homo sapiens 213-216 16852147-7 2005 This approach was used to study the catalytic decomposition of hydrogen peroxide (HO2- --> 1/2O2 + OH-), where nu(S) = 0.5, on supported catalysts. Hydrogen Peroxide 63-80 heme oxygenase 2 Homo sapiens 82-85 16852147-8 2005 A gold-mercury amalgam tip was used to quantitatively reduce dissolved O2 (mediator) to HO2-, which was decomposed back to oxygen at the catalyst substrate. Mercury 7-14 heme oxygenase 2 Homo sapiens 88-91 16852147-8 2005 A gold-mercury amalgam tip was used to quantitatively reduce dissolved O2 (mediator) to HO2-, which was decomposed back to oxygen at the catalyst substrate. Oxygen 71-73 heme oxygenase 2 Homo sapiens 88-91 16852147-8 2005 A gold-mercury amalgam tip was used to quantitatively reduce dissolved O2 (mediator) to HO2-, which was decomposed back to oxygen at the catalyst substrate. Oxygen 123-129 heme oxygenase 2 Homo sapiens 88-91 15918699-6 2005 The determined structure is planar and almost T shaped, where the argon atom is slightly shifted to the hydrogen atom of HO2. Hydrogen 104-112 heme oxygenase 2 Homo sapiens 121-124 15377391-0 2004 Heme oxygenase-2 gene deletion attenuates oxidative stress in neurons exposed to extracellular hemin. Hemin 95-100 heme oxygenase 2 Homo sapiens 0-16 16833643-0 2005 Water dependence of the HO2 self reaction: kinetics of the HO2-H2O complex. Water 0-5 heme oxygenase 2 Homo sapiens 24-27 16833643-0 2005 Water dependence of the HO2 self reaction: kinetics of the HO2-H2O complex. Water 0-5 heme oxygenase 2 Homo sapiens 59-62 16833643-0 2005 Water dependence of the HO2 self reaction: kinetics of the HO2-H2O complex. Water 63-66 heme oxygenase 2 Homo sapiens 24-27 16833643-0 2005 Water dependence of the HO2 self reaction: kinetics of the HO2-H2O complex. Water 63-66 heme oxygenase 2 Homo sapiens 59-62 16833643-1 2005 Transient absorption spectra and decay profiles of HO2 have been measured using cw near-IR two-tone frequency modulation absorption spectroscopy at 297 K and 50 Torr in diluent of N2 in the presence of water. Nitrogen 180-182 heme oxygenase 2 Homo sapiens 51-54 16833643-1 2005 Transient absorption spectra and decay profiles of HO2 have been measured using cw near-IR two-tone frequency modulation absorption spectroscopy at 297 K and 50 Torr in diluent of N2 in the presence of water. Water 202-207 heme oxygenase 2 Homo sapiens 51-54 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 77-82 heme oxygenase 2 Homo sapiens 26-29 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 77-82 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 77-82 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 77-82 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 77-82 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 77-82 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 131-134 heme oxygenase 2 Homo sapiens 26-29 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 131-134 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 131-134 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 131-134 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 131-134 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 131-134 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 150-153 heme oxygenase 2 Homo sapiens 26-29 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 150-153 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 150-153 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 150-153 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 150-153 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 150-153 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 256-261 heme oxygenase 2 Homo sapiens 26-29 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 256-261 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 256-261 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 256-261 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 256-261 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Water 256-261 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Nitrogen 440-442 heme oxygenase 2 Homo sapiens 26-29 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Nitrogen 440-442 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Nitrogen 440-442 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Nitrogen 440-442 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Nitrogen 440-442 heme oxygenase 2 Homo sapiens 125-128 16833643-2 2005 From the depletion of the HO2 absorption peak area following the addition of water, the equilibrium constant of the reaction HO2 + H2O <--> HO2-H2O was determined to be K2 = (5.2 +/- 3.2) x 10(-19) cm3 molecule(-1) at 297 K. Substituting K2 into the water dependence of the HO2 decay rate, the rate coefficient of the reaction HO2 + HO2-H2O was estimated to be (1.5 +/- 0.1) x 10(-11) cm3 molecule(-1) s(-1) at 297 K and 50 Torr with N2 as the diluent. Nitrogen 440-442 heme oxygenase 2 Homo sapiens 125-128 16833643-3 2005 This reaction is much faster than the HO2 self-reaction without water. Water 64-69 heme oxygenase 2 Homo sapiens 38-41 16833643-4 2005 It is suggested that the apparent rate of the HO2 self-reaction is enhanced by the formation of the HO2-H2O complex and its subsequent reaction. Water 104-107 heme oxygenase 2 Homo sapiens 46-49 16833643-4 2005 It is suggested that the apparent rate of the HO2 self-reaction is enhanced by the formation of the HO2-H2O complex and its subsequent reaction. Water 104-107 heme oxygenase 2 Homo sapiens 100-103 16833643-5 2005 Results are discussed with respect to the kinetics and atmospheric chemistry of the HO2-H2O complex. Water 88-91 heme oxygenase 2 Homo sapiens 84-87 16833643-6 2005 At 297 K and 50% humidity, the concentration ratio of [HO2-H2O]/[HO2] was estimated from the value of K2 to be 0.19 +/- 0.11. Water 59-62 heme oxygenase 2 Homo sapiens 55-58 16833414-4 2005 Hydrogen abstraction to form HO2 + SH is the dominant product channel and proceeds through a loose transition state well-described at the level of calculation employed. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 29-32 19785156-1 2005 The reaction of HO2 with toluene and kerosene flame soot was studied over the temperature range 240-350 K and at P = 0.5-5 Torr of helium using a discharge flow reactor coupled to a modulated molecular beam mass spectrometer. Toluene 25-32 heme oxygenase 2 Homo sapiens 16-19 19785156-1 2005 The reaction of HO2 with toluene and kerosene flame soot was studied over the temperature range 240-350 K and at P = 0.5-5 Torr of helium using a discharge flow reactor coupled to a modulated molecular beam mass spectrometer. Helium 131-137 heme oxygenase 2 Homo sapiens 16-19 19785156-3 2005 The independent of temperature in the range 240-350 K value of gamma = (7.5 +/- 1.5) x 10(-2) (calculated with geometric surface area) was found for the uptake coefficient of HO2 on kerosene and toluene soot. Toluene 195-202 heme oxygenase 2 Homo sapiens 175-178 19785156-6 2005 The results show that the HO2 + soot reaction could be a significant loss process for HOx in the urban atmosphere with a potential impact on photochemical ozone formation. hydrogen oxalate 86-89 heme oxygenase 2 Homo sapiens 26-29 16158592-7 2005 HO2 may promote organic compounds oxidized in WAO of the apramycin wastewater. apramycin 57-66 heme oxygenase 2 Homo sapiens 0-3 16851983-0 2005 Measurements and modeling of HO2 formation in the reactions of n-C3H7 and i-C3H7 radicals with O2. Propyl radical 63-69 heme oxygenase 2 Homo sapiens 29-32 16851983-0 2005 Measurements and modeling of HO2 formation in the reactions of n-C3H7 and i-C3H7 radicals with O2. i-c3h7 74-80 heme oxygenase 2 Homo sapiens 29-32 15377391-12 2004 CONCLUSIONS: These results suggest that HO-2 gene deletion protects neurons in mixed neuron-astrocyte cultures from heme-mediated oxidative injury. Heme 116-120 heme oxygenase 2 Homo sapiens 40-44 15377391-3 2004 In a prior study, heme oxygenase-2 gene deletion increased the vulnerability of cultured cortical astrocytes to hemin. Hemin 112-117 heme oxygenase 2 Homo sapiens 18-34 15053633-5 2004 But the large KIE found in peroxone: HPR-O3/DPR-O3 = 19.6 +/- 4.0, is due to an elementary (O3 + HO2-) reaction involving H-O2- bond cleavage. peroxone 27-35 heme oxygenase 2 Homo sapiens 97-100 15260334-5 2004 The main influence of the scavenger arises from its independent production of HO2 radicals, with CO producing the most HO2, 2-butanol an intermediate amount, and cyclohexane the least. 2-butanol 124-133 heme oxygenase 2 Homo sapiens 78-81 15260334-5 2004 The main influence of the scavenger arises from its independent production of HO2 radicals, with CO producing the most HO2, 2-butanol an intermediate amount, and cyclohexane the least. Cyclohexane 162-173 heme oxygenase 2 Homo sapiens 78-81 15303850-0 2004 Tropopause chemistry revisited: HO2*-initiated oxidation as an efficient acetone sink. Acetone 73-80 heme oxygenase 2 Homo sapiens 32-35 15303850-2 2004 In this theoretical study, using amply validated methodologies, the hitherto overlooked reaction of acetone with HO2* radicals is found to lead to a fast equilibrium (CH3)2C=O + HO2* right harpoon over left harpoon (CH3)2C(OH)OO*. Acetone 100-107 heme oxygenase 2 Homo sapiens 113-116 15303850-2 2004 In this theoretical study, using amply validated methodologies, the hitherto overlooked reaction of acetone with HO2* radicals is found to lead to a fast equilibrium (CH3)2C=O + HO2* right harpoon over left harpoon (CH3)2C(OH)OO*. Acetone 100-107 heme oxygenase 2 Homo sapiens 178-181 15175337-6 2004 Calmodulin binds with nanomolar affinity to HO2 in a calcium-dependent manner via a canonical 1-10 motif, resulting in a 3-fold increase in catalytic activity. Calcium 53-60 heme oxygenase 2 Homo sapiens 44-47 15175337-8 2004 The calcium mobilizing agents ionomycin and glutamate stimulate endogenous HO2 activity in primary cortical cultures, establishing in vivo relevance. Calcium 4-11 heme oxygenase 2 Homo sapiens 75-78 15175337-8 2004 The calcium mobilizing agents ionomycin and glutamate stimulate endogenous HO2 activity in primary cortical cultures, establishing in vivo relevance. Ionomycin 30-39 heme oxygenase 2 Homo sapiens 75-78 15175337-8 2004 The calcium mobilizing agents ionomycin and glutamate stimulate endogenous HO2 activity in primary cortical cultures, establishing in vivo relevance. Glutamic Acid 44-53 heme oxygenase 2 Homo sapiens 75-78 15053633-7 2004 +.O2-, would emerge as a KIE1/2 factor in the rates of the ensuing radical chain, the magnitude of the observed KIE must be associated with the hydride transfer reaction that yields a diamagnetic species: O3 + HO2- HO3- + O2. Oxygen 2-4 heme oxygenase 2 Homo sapiens 210-213 15053633-7 2004 +.O2-, would emerge as a KIE1/2 factor in the rates of the ensuing radical chain, the magnitude of the observed KIE must be associated with the hydride transfer reaction that yields a diamagnetic species: O3 + HO2- HO3- + O2. Ozone 205-209 heme oxygenase 2 Homo sapiens 210-213 14983060-1 2004 Carbon monoxide (CO) synthesized by heme oxygenase 2 (HO2) and nitric oxide (NO) produced by neuronal NO synthase (nNOS) mediate nonadrenergic/noncholinergic (NANC) intestinal relaxation. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 36-52 15069378-4 2004 HO-2 is a constitutive enzyme involved in the baseline production of CO in the cardiovascular and nervous systems, whereas HO-3 is also ubiquitously expressed, but possesses low catalytic activity. Carbon Monoxide 69-71 heme oxygenase 2 Homo sapiens 0-4 15012112-2 2004 Recent studies have suggested that hydroperoxy radicals (HO2) have an affinity for binding to a water surface. perhydroxyl radical 35-55 heme oxygenase 2 Homo sapiens 57-60 15012112-2 2004 Recent studies have suggested that hydroperoxy radicals (HO2) have an affinity for binding to a water surface. Water 96-101 heme oxygenase 2 Homo sapiens 57-60 15012112-4 2004 The analyses reveal that, for the binding of an HO2 radical to a water surface, the two water molecules nearest the radical are the most relevant to the bonding and the addition of other water molecules has little affect on the bonding between the radical and the two nearest waters. Water 65-70 heme oxygenase 2 Homo sapiens 48-51 15012112-4 2004 The analyses reveal that, for the binding of an HO2 radical to a water surface, the two water molecules nearest the radical are the most relevant to the bonding and the addition of other water molecules has little affect on the bonding between the radical and the two nearest waters. Water 88-93 heme oxygenase 2 Homo sapiens 48-51 15012112-4 2004 The analyses reveal that, for the binding of an HO2 radical to a water surface, the two water molecules nearest the radical are the most relevant to the bonding and the addition of other water molecules has little affect on the bonding between the radical and the two nearest waters. Water 88-93 heme oxygenase 2 Homo sapiens 48-51 14983060-1 2004 Carbon monoxide (CO) synthesized by heme oxygenase 2 (HO2) and nitric oxide (NO) produced by neuronal NO synthase (nNOS) mediate nonadrenergic/noncholinergic (NANC) intestinal relaxation. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 54-57 14983060-1 2004 Carbon monoxide (CO) synthesized by heme oxygenase 2 (HO2) and nitric oxide (NO) produced by neuronal NO synthase (nNOS) mediate nonadrenergic/noncholinergic (NANC) intestinal relaxation. Carbon Monoxide 17-19 heme oxygenase 2 Homo sapiens 36-52 14983060-1 2004 Carbon monoxide (CO) synthesized by heme oxygenase 2 (HO2) and nitric oxide (NO) produced by neuronal NO synthase (nNOS) mediate nonadrenergic/noncholinergic (NANC) intestinal relaxation. Carbon Monoxide 17-19 heme oxygenase 2 Homo sapiens 54-57 14983060-5 2004 By using a combination of pharmacology and genetic knockout of the biosynthetic enzymes for CO and NO, we show that the physiologic effects of exogenous and endogenous VIP in the IAS are mediated by HO2-synthesized CO. Carbon Monoxide 92-94 heme oxygenase 2 Homo sapiens 199-202 14983060-5 2004 By using a combination of pharmacology and genetic knockout of the biosynthetic enzymes for CO and NO, we show that the physiologic effects of exogenous and endogenous VIP in the IAS are mediated by HO2-synthesized CO. Carbon Monoxide 215-217 heme oxygenase 2 Homo sapiens 199-202 14562166-1 2003 INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). Heme 80-84 heme oxygenase 2 Homo sapiens 54-58 14653685-2 2003 The cleavage by HO2(-) proceeds faster than by OH(-) and involves additional routes with general acid assistance by H2O2 and general base assistance by OH(-) and HO2(-). Hydrogen Peroxide 116-120 heme oxygenase 2 Homo sapiens 16-19 14615405-6 2003 Preexposure (24 h) in a combination of low O2 and low glucose concentrations decreased the protein content of the HO-1 isoform by 59.6% (P < 0.05), whereas preexposure (24 h) to low glucose concentration alone increased HO-2 content by 28.2% in chorionic villi explants (P < 0.05). Glucose 54-61 heme oxygenase 2 Homo sapiens 223-227 14562166-1 2003 INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). Carbon Monoxide 124-126 heme oxygenase 2 Homo sapiens 54-58 14562166-1 2003 INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). Iron 98-102 heme oxygenase 2 Homo sapiens 54-58 14562166-1 2003 INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). Carbon Monoxide 107-122 heme oxygenase 2 Homo sapiens 54-58 14632084-1 2003 The hydroperoxyl radical (HO2) is one of the most abundant free radicals in the atmosphere, where it participates in a series of photochemical reactions that determine the fate of natural and anthropogenic emissions. Hydroperoxy radical 4-24 heme oxygenase 2 Homo sapiens 26-29 14710808-3 2003 Peroxy radicals (HO2 and RO2) within this air are detected by amplified chemical conversion into a unique ion (HSO4-) via the chemistry initiated by the addition of NO and SO2 to the inlet. peroxy radicals 0-15 heme oxygenase 2 Homo sapiens 17-20 14710808-3 2003 Peroxy radicals (HO2 and RO2) within this air are detected by amplified chemical conversion into a unique ion (HSO4-) via the chemistry initiated by the addition of NO and SO2 to the inlet. hso4 111-115 heme oxygenase 2 Homo sapiens 17-20 14710808-3 2003 Peroxy radicals (HO2 and RO2) within this air are detected by amplified chemical conversion into a unique ion (HSO4-) via the chemistry initiated by the addition of NO and SO2 to the inlet. Sulfur Dioxide 172-175 heme oxygenase 2 Homo sapiens 17-20 14703794-10 2003 We also suggest that many of the allegedly O2*- dependent bacterial pathologies and carcinogenic derailments are due to membrane-modifying activity rather than other chemical reactions of O2*-/HO2*. Superoxides 43-45 heme oxygenase 2 Homo sapiens 193-196 12946226-3 2003 Heme oxygenase-2 (HO-2) is the major physiological mechanism for the generation of carbon monoxide in the enteric nervous system. Carbon Monoxide 83-98 heme oxygenase 2 Homo sapiens 0-16 12946226-3 2003 Heme oxygenase-2 (HO-2) is the major physiological mechanism for the generation of carbon monoxide in the enteric nervous system. Carbon Monoxide 83-98 heme oxygenase 2 Homo sapiens 18-22 14527438-0 2003 Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 70-86 14527438-3 2003 Phorbol ester treatment of hippocampal cultures results in the phosphorylation and activation of HO2 by CK2, implicating protein kinase C (PKC) in CK2 stimulation. Phorbol Esters 0-13 heme oxygenase 2 Homo sapiens 97-100 14632084-1 2003 The hydroperoxyl radical (HO2) is one of the most abundant free radicals in the atmosphere, where it participates in a series of photochemical reactions that determine the fate of natural and anthropogenic emissions. Free Radicals 59-72 heme oxygenase 2 Homo sapiens 26-29 14632084-2 2003 In addition, HO2 is found in droplets and surface water as a result of photochemical formation and gas-phase scavenging. Water 50-55 heme oxygenase 2 Homo sapiens 13-16 14632084-3 2003 We describe a quantitative method for determining trace concentrations of HO2 radicals that exploits the chemiluminescence produced upon reaction with a synthetic analogue of luciferin from the crustacean Cypridina. D-luciferin 175-184 heme oxygenase 2 Homo sapiens 74-77 14632084-4 2003 The technique is linear at least up to 1 microM HO2(aq) and has a minimum detection limit of 0.1 nM. aq 52-54 heme oxygenase 2 Homo sapiens 48-51 12767239-0 2003 Identification of the internal axial ligand of HO2-cobalt(III)-bleomycin: 1H[15N] HSQC NMR investigation of bleomycin, deglycobleomycin, and their hydroperoxide-cobalt(III) complexes. Hydrogen 74-76 heme oxygenase 2 Homo sapiens 47-50 14506930-1 2003 PROBLEM: We previously reported a diminished expression of the heme-degrading enzymes heme oxygenases (HO)-1 and HO-2 in decidua and placenta from mice undergoing Th1-mediated abortion, strongly indicating the protective effect of HO in murine pregnancy maintenance. Heme 63-67 heme oxygenase 2 Homo sapiens 113-117 14506930-9 2003 CONCLUSIONS: Our data indicate that HOs play a crucial role in pregnancy and low expression of HO-2, as observed in pathologic pregnancies, may lead to enhanced levels of free heme at the feto-maternal interface, with subsequent upregulation of adhesion molecules, allowing enhanced inflammatory cells migration to the feto-maternal interface. Heme 176-180 heme oxygenase 2 Homo sapiens 95-99 12767239-0 2003 Identification of the internal axial ligand of HO2-cobalt(III)-bleomycin: 1H[15N] HSQC NMR investigation of bleomycin, deglycobleomycin, and their hydroperoxide-cobalt(III) complexes. Hydrogen Peroxide 147-160 heme oxygenase 2 Homo sapiens 47-50 12767239-0 2003 Identification of the internal axial ligand of HO2-cobalt(III)-bleomycin: 1H[15N] HSQC NMR investigation of bleomycin, deglycobleomycin, and their hydroperoxide-cobalt(III) complexes. cobalt(iii) 51-62 heme oxygenase 2 Homo sapiens 47-50 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Heme 0-4 heme oxygenase 2 Homo sapiens 97-101 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Biliverdine 123-133 heme oxygenase 2 Homo sapiens 97-101 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Bilirubin 134-143 heme oxygenase 2 Homo sapiens 97-101 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Carbon Monoxide 145-147 heme oxygenase 2 Homo sapiens 97-101 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Iron 153-157 heme oxygenase 2 Homo sapiens 97-101 14580148-4 2003 Characteristically, human HO-1 contains no Cys residues, whereas HO-2 contains the potential heme-binding motifs of the Cys-Pro dipeptide. Heme 93-97 heme oxygenase 2 Homo sapiens 65-69 14580148-4 2003 Characteristically, human HO-1 contains no Cys residues, whereas HO-2 contains the potential heme-binding motifs of the Cys-Pro dipeptide. cysteinylproline 120-127 heme oxygenase 2 Homo sapiens 65-69 14580148-4 2003 Characteristically, human HO-1 contains no Cys residues, whereas HO-2 contains the potential heme-binding motifs of the Cys-Pro dipeptide. Dipeptides 128-137 heme oxygenase 2 Homo sapiens 65-69 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Glutamic Acid 38-47 heme oxygenase 2 Homo sapiens 100-116 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Glutamic Acid 38-47 heme oxygenase 2 Homo sapiens 118-122 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Carbon Monoxide 57-72 heme oxygenase 2 Homo sapiens 100-116 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Carbon Monoxide 57-72 heme oxygenase 2 Homo sapiens 118-122 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Carbon Monoxide 74-76 heme oxygenase 2 Homo sapiens 100-116 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Carbon Monoxide 74-76 heme oxygenase 2 Homo sapiens 118-122 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Heme 92-96 heme oxygenase 2 Homo sapiens 100-116 12623781-1 2003 Dilation of piglet pial arterioles to glutamate involves carbon monoxide (CO) produced from heme by heme oxygenase-2 (HO-2). Heme 92-96 heme oxygenase 2 Homo sapiens 118-122 12623781-2 2003 Piglet cerebral microvessels and endothelial and smooth muscle cells grown on microcarrier beads were used to address the hypothesis that glutamate increases endothelial CO production by increasing HO-2 catalytic activity. Glutamic Acid 138-147 heme oxygenase 2 Homo sapiens 198-202 12623781-9 2003 The mechanism of HO-2 stimulation by glutamate appears to be independent of cytosolic Ca, because stimulation of CO production by glutamate was the same in Careplete medium, Ca-free medium with ionomycin, and Careplete medium with ionomycin. Glutamic Acid 37-46 heme oxygenase 2 Homo sapiens 17-21 12623781-9 2003 The mechanism of HO-2 stimulation by glutamate appears to be independent of cytosolic Ca, because stimulation of CO production by glutamate was the same in Careplete medium, Ca-free medium with ionomycin, and Careplete medium with ionomycin. Glutamic Acid 130-139 heme oxygenase 2 Homo sapiens 17-21 12623781-9 2003 The mechanism of HO-2 stimulation by glutamate appears to be independent of cytosolic Ca, because stimulation of CO production by glutamate was the same in Careplete medium, Ca-free medium with ionomycin, and Careplete medium with ionomycin. Ionomycin 194-203 heme oxygenase 2 Homo sapiens 17-21 12623781-9 2003 The mechanism of HO-2 stimulation by glutamate appears to be independent of cytosolic Ca, because stimulation of CO production by glutamate was the same in Careplete medium, Ca-free medium with ionomycin, and Careplete medium with ionomycin. Ionomycin 231-240 heme oxygenase 2 Homo sapiens 17-21 12623781-10 2003 Therefore, glutamate appears to increase HO-2 catalytic activity in cerebral microvessels via a tyrosine kinase mediated pathway. Glutamic Acid 11-20 heme oxygenase 2 Homo sapiens 41-45 12767239-0 2003 Identification of the internal axial ligand of HO2-cobalt(III)-bleomycin: 1H[15N] HSQC NMR investigation of bleomycin, deglycobleomycin, and their hydroperoxide-cobalt(III) complexes. 15n 77-80 heme oxygenase 2 Homo sapiens 47-50 12767239-0 2003 Identification of the internal axial ligand of HO2-cobalt(III)-bleomycin: 1H[15N] HSQC NMR investigation of bleomycin, deglycobleomycin, and their hydroperoxide-cobalt(III) complexes. Bleomycin 63-72 heme oxygenase 2 Homo sapiens 47-50 12767239-0 2003 Identification of the internal axial ligand of HO2-cobalt(III)-bleomycin: 1H[15N] HSQC NMR investigation of bleomycin, deglycobleomycin, and their hydroperoxide-cobalt(III) complexes. deglycobleomycin 119-135 heme oxygenase 2 Homo sapiens 47-50 12926365-5 2003 Addition of .OH to phenol gives rise to dihydroxycyclohexadienyl radicals which add dioxygen and eliminate HO2. Phenol 19-25 heme oxygenase 2 Homo sapiens 107-110 12926365-5 2003 Addition of .OH to phenol gives rise to dihydroxycyclohexadienyl radicals which add dioxygen and eliminate HO2. dihydroxycyclohexadienyl radicals 40-73 heme oxygenase 2 Homo sapiens 107-110 12926365-5 2003 Addition of .OH to phenol gives rise to dihydroxycyclohexadienyl radicals which add dioxygen and eliminate HO2. Oxygen 84-92 heme oxygenase 2 Homo sapiens 107-110 12553769-8 2003 The ECL peak at 1.54 V was suggested to be due to the electrooxidation of OH- to HO2- at higher potential and then to O2-, which reacted with luminol to produce light emission. Luminol 142-149 heme oxygenase 2 Homo sapiens 81-84 12578814-5 2003 HO-2 protein content was decreased by 17% and 5% in human trophoblast cells after 24-h exposure to 1% and 5% O(2), respectively, versus 20% O(2). o(2) 109-113 heme oxygenase 2 Homo sapiens 0-4 12578814-5 2003 HO-2 protein content was decreased by 17% and 5% in human trophoblast cells after 24-h exposure to 1% and 5% O(2), respectively, versus 20% O(2). o(2) 140-144 heme oxygenase 2 Homo sapiens 0-4 12785056-10 2003 The various functions of oxygen, e.g. (1) quenching of the triplet state; (2) quenching of the semiquinone radical, thereby forming HO2*/O2*- radicals; and (3) trapping of the dihydroxyanthracenes are outlined. Oxygen 25-31 heme oxygenase 2 Homo sapiens 132-135 12553769-10 2003 At -0.58 V, the dissolved oxygen in solution was reduced to HO2-, resulting in light emission. Oxygen 26-32 heme oxygenase 2 Homo sapiens 60-63 12298195-4 2002 interacts with lysine to form a thermodynamically stable complex with proton transfer and formation of the HO2. Lysine 15-21 heme oxygenase 2 Homo sapiens 107-110 12964953-5 2003 HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO). Bilirubin 143-160 heme oxygenase 2 Homo sapiens 47-63 12964953-5 2003 HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO). Iron 170-174 heme oxygenase 2 Homo sapiens 47-63 12964953-5 2003 HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO). Carbon Monoxide 180-195 heme oxygenase 2 Homo sapiens 47-63 12964953-5 2003 HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO). Carbon Monoxide 197-199 heme oxygenase 2 Homo sapiens 47-63 12758020-7 2003 Atmospheric OH and HO2 concentrations and the NOx/HO2 ratio were identified as the governing quantities controlling the TCA formation trough methyl chloroform oxidation in the gas phase. Trichloroacetic Acid 120-123 heme oxygenase 2 Homo sapiens 19-22 12758020-7 2003 Atmospheric OH and HO2 concentrations and the NOx/HO2 ratio were identified as the governing quantities controlling the TCA formation trough methyl chloroform oxidation in the gas phase. Trichloroacetic Acid 120-123 heme oxygenase 2 Homo sapiens 50-53 12758020-7 2003 Atmospheric OH and HO2 concentrations and the NOx/HO2 ratio were identified as the governing quantities controlling the TCA formation trough methyl chloroform oxidation in the gas phase. 1,1,1-trichloroethane 141-158 heme oxygenase 2 Homo sapiens 19-22 12758020-7 2003 Atmospheric OH and HO2 concentrations and the NOx/HO2 ratio were identified as the governing quantities controlling the TCA formation trough methyl chloroform oxidation in the gas phase. 1,1,1-trichloroethane 141-158 heme oxygenase 2 Homo sapiens 50-53 12592623-3 2003 Heme oxygenase-2 (HO-2) is the main physiologic mechanism for generating CO in human cells. Carbon Monoxide 73-75 heme oxygenase 2 Homo sapiens 0-16 12592623-3 2003 Heme oxygenase-2 (HO-2) is the main physiologic mechanism for generating CO in human cells. Carbon Monoxide 73-75 heme oxygenase 2 Homo sapiens 18-22 11909697-2 2002 Several studies have been published on the localization of the carbon monoxide producing enzyme heme oxygenase-2 (HO-2), which concomitantly generates biliverdin; histochemical data on the distribution of biliverdin reductase (BVR), converting biliverdin to bilirubin, are still very scarce in large mammals including humans. Carbon Monoxide 63-78 heme oxygenase 2 Homo sapiens 96-112 12042065-1 2002 HO2*, usually termed either hydroperoxyl radical or perhydroxyl radical, is the protonated form of superoxide; the protonation/deprotonation equilibrium exhibits a pK(a) of around 4.8. Hydroperoxy radical 28-48 heme oxygenase 2 Homo sapiens 0-3 12042065-1 2002 HO2*, usually termed either hydroperoxyl radical or perhydroxyl radical, is the protonated form of superoxide; the protonation/deprotonation equilibrium exhibits a pK(a) of around 4.8. perhydroxyl radical 52-71 heme oxygenase 2 Homo sapiens 0-3 12042065-1 2002 HO2*, usually termed either hydroperoxyl radical or perhydroxyl radical, is the protonated form of superoxide; the protonation/deprotonation equilibrium exhibits a pK(a) of around 4.8. Superoxides 99-109 heme oxygenase 2 Homo sapiens 0-3 11909697-2 2002 Several studies have been published on the localization of the carbon monoxide producing enzyme heme oxygenase-2 (HO-2), which concomitantly generates biliverdin; histochemical data on the distribution of biliverdin reductase (BVR), converting biliverdin to bilirubin, are still very scarce in large mammals including humans. Carbon Monoxide 63-78 heme oxygenase 2 Homo sapiens 114-118 11909697-2 2002 Several studies have been published on the localization of the carbon monoxide producing enzyme heme oxygenase-2 (HO-2), which concomitantly generates biliverdin; histochemical data on the distribution of biliverdin reductase (BVR), converting biliverdin to bilirubin, are still very scarce in large mammals including humans. Biliverdine 151-161 heme oxygenase 2 Homo sapiens 96-112 11909697-2 2002 Several studies have been published on the localization of the carbon monoxide producing enzyme heme oxygenase-2 (HO-2), which concomitantly generates biliverdin; histochemical data on the distribution of biliverdin reductase (BVR), converting biliverdin to bilirubin, are still very scarce in large mammals including humans. Biliverdine 151-161 heme oxygenase 2 Homo sapiens 114-118 11592948-6 2001 Both desferrioxamine and CoCl(2) markedly increased HIF-1alpha mRNA and protein levels and resulted in the upregulation of HO-1 mRNA but not HO-2. Deferoxamine 5-20 heme oxygenase 2 Homo sapiens 141-145 15499991-3 2002 Three isoforms of heme oxygenase (HO) have been described: two constitutively expressed isoforms, HO-2 and HO-3, and an inducible isoform, HO-1 that is increased as an adaptive response to several injurious stimuli including heme, hyperoxia, hypoxia, endotoxin and heavy metals. Heme 18-22 heme oxygenase 2 Homo sapiens 98-102 12025512-3 2002 Voltammetric tests, combined with coulometric and spectrophotometric measurements, pointed out that each mol of curcumin is able to react with six mols of such anion radical, through a process initiated by an acid-base step, which provides the perhydroxyl radical, HO2. Curcumin 112-120 heme oxygenase 2 Homo sapiens 265-268 12025512-3 2002 Voltammetric tests, combined with coulometric and spectrophotometric measurements, pointed out that each mol of curcumin is able to react with six mols of such anion radical, through a process initiated by an acid-base step, which provides the perhydroxyl radical, HO2. anion radical 160-173 heme oxygenase 2 Homo sapiens 265-268 12025512-3 2002 Voltammetric tests, combined with coulometric and spectrophotometric measurements, pointed out that each mol of curcumin is able to react with six mols of such anion radical, through a process initiated by an acid-base step, which provides the perhydroxyl radical, HO2. perhydroxyl radical 244-263 heme oxygenase 2 Homo sapiens 265-268 11592948-6 2001 Both desferrioxamine and CoCl(2) markedly increased HIF-1alpha mRNA and protein levels and resulted in the upregulation of HO-1 mRNA but not HO-2. cobaltous chloride 25-32 heme oxygenase 2 Homo sapiens 141-145 11592948-7 2001 Furthermore, inhibition of HIF-1alpha degradation by CBZ-LLL, an inhibitor of ubiquitin-proteasome, significantly increased HIF-1alpha protein and HO-1 mRNA but not HO-2 in these cells. carbobenzoxy-leucyl-leucyl-leucine 53-60 heme oxygenase 2 Homo sapiens 165-169 11554454-5 2001 Spectral analyses, using 1:4 or 1:1 molar ratio of the heme to 10-residue peptides, corresponding to HRM containing HO-2 sequences, revealed specific interactions as indicated by a shift in the absorption spectrum of heme. Heme 55-59 heme oxygenase 2 Homo sapiens 116-120 11572959-3 2001 The constitutive forms of the enzyme are differentially activated, with calcium entry stimulating NOS by binding to calmodulin, whereas calcium entry activates protein kinase C to phosphorylate and activate HO2. Calcium 136-143 heme oxygenase 2 Homo sapiens 207-210 11572959-11 2001 On the other hand, massive neuronal firing during a stroke presumably activates HO2, leading to neuroprotective actions of bilirubin. Bilirubin 123-132 heme oxygenase 2 Homo sapiens 80-83 11554454-0 2001 Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs. Metalloporphyrins 34-51 heme oxygenase 2 Homo sapiens 0-16 11554454-0 2001 Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs. Heme 65-69 heme oxygenase 2 Homo sapiens 0-16 11531124-1 2001 The mechanism of the gas-phase reaction of *CH2OH+O2 to form CH2O+HO2* was studied theoretically by means of high-level quantum-chemical electronic structure methods (CASSCF and CCSD(T)). Hydroxymethyl radical 44-49 heme oxygenase 2 Homo sapiens 66-69 11531124-1 2001 The mechanism of the gas-phase reaction of *CH2OH+O2 to form CH2O+HO2* was studied theoretically by means of high-level quantum-chemical electronic structure methods (CASSCF and CCSD(T)). Oxygen 50-52 heme oxygenase 2 Homo sapiens 66-69 11531124-1 2001 The mechanism of the gas-phase reaction of *CH2OH+O2 to form CH2O+HO2* was studied theoretically by means of high-level quantum-chemical electronic structure methods (CASSCF and CCSD(T)). Formaldehyde 44-48 heme oxygenase 2 Homo sapiens 66-69 11531124-3 2001 The concerted elimination of HO2* from 1 is predicted to occur via a five-membered ringlike transition structure of Cs symmetry, TS1, which lies 19.6 kcalmol(-1) below the sum of the energies of the reactants at 0 K. A four-membered ringlike transition structure TS2 of Cs symmetry, which lies 13.9 kcalmol(-1) above the energy of the separated reactants at 0 K, was also found for the concerted HO2* elimination from 1. Cesium 116-118 heme oxygenase 2 Homo sapiens 29-32 11531124-3 2001 The concerted elimination of HO2* from 1 is predicted to occur via a five-membered ringlike transition structure of Cs symmetry, TS1, which lies 19.6 kcalmol(-1) below the sum of the energies of the reactants at 0 K. A four-membered ringlike transition structure TS2 of Cs symmetry, which lies 13.9 kcalmol(-1) above the energy of the separated reactants at 0 K, was also found for the concerted HO2* elimination from 1. Cesium 116-118 heme oxygenase 2 Homo sapiens 396-399 11531124-3 2001 The concerted elimination of HO2* from 1 is predicted to occur via a five-membered ringlike transition structure of Cs symmetry, TS1, which lies 19.6 kcalmol(-1) below the sum of the energies of the reactants at 0 K. A four-membered ringlike transition structure TS2 of Cs symmetry, which lies 13.9 kcalmol(-1) above the energy of the separated reactants at 0 K, was also found for the concerted HO2* elimination from 1. Cesium 270-272 heme oxygenase 2 Homo sapiens 29-32 11531124-6 2001 The observed non-Arrhenius behavior of the temperature dependence of the rate constant for the gas-phase oxidation of *CH2OH is ascribed to the combined effect of the initial barrier-free formation of the *OO-CH2OH adduct with a substantial energy release and the existence of a low-barrier and two high-barrier pathways for its decomposition into CH2O and HO2*. Hydroxymethyl radical 119-124 heme oxygenase 2 Homo sapiens 357-360 11531124-6 2001 The observed non-Arrhenius behavior of the temperature dependence of the rate constant for the gas-phase oxidation of *CH2OH is ascribed to the combined effect of the initial barrier-free formation of the *OO-CH2OH adduct with a substantial energy release and the existence of a low-barrier and two high-barrier pathways for its decomposition into CH2O and HO2*. Hydroxymethyl radical 209-214 heme oxygenase 2 Homo sapiens 357-360 11531124-6 2001 The observed non-Arrhenius behavior of the temperature dependence of the rate constant for the gas-phase oxidation of *CH2OH is ascribed to the combined effect of the initial barrier-free formation of the *OO-CH2OH adduct with a substantial energy release and the existence of a low-barrier and two high-barrier pathways for its decomposition into CH2O and HO2*. Formaldehyde 119-123 heme oxygenase 2 Homo sapiens 357-360 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. Heme 33-37 heme oxygenase 2 Homo sapiens 0-16 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. Heme 33-37 heme oxygenase 2 Homo sapiens 18-22 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. ferriheme b(1-) 39-59 heme oxygenase 2 Homo sapiens 0-16 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. ferriheme b(1-) 39-59 heme oxygenase 2 Homo sapiens 18-22 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. fe-pp 61-66 heme oxygenase 2 Homo sapiens 0-16 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. fe-pp 61-66 heme oxygenase 2 Homo sapiens 18-22 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. Carbon Monoxide 72-74 heme oxygenase 2 Homo sapiens 0-16 11554454-5 2001 Spectral analyses, using 1:4 or 1:1 molar ratio of the heme to 10-residue peptides, corresponding to HRM containing HO-2 sequences, revealed specific interactions as indicated by a shift in the absorption spectrum of heme. Heme 217-221 heme oxygenase 2 Homo sapiens 116-120 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. Carbon Monoxide 72-74 heme oxygenase 2 Homo sapiens 18-22 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. Bilirubin 79-88 heme oxygenase 2 Homo sapiens 0-16 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Heme 49-53 heme oxygenase 2 Homo sapiens 44-48 11554454-1 2001 Heme oxygenase-2 (HO-2) degrades heme [Fe-protoporphyrin IX (Fe-PP)] to CO and bilirubin. Bilirubin 79-88 heme oxygenase 2 Homo sapiens 18-22 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Heme 71-75 heme oxygenase 2 Homo sapiens 44-48 11554454-3 2001 HO-2 has two copies of heme regulatory motif (HRM) with a conserved core of Cys264-Pro265 and Cys281-Pro282. Heme 23-27 heme oxygenase 2 Homo sapiens 0-4 11554454-4 2001 We examined interaction of HO-2 HRMs with Fe-PP, Zn-protoporphyrin IX (Zn-PP; HO-2 inhibitor), and protoporphyrin IX (PP IX). fe-pp 42-47 heme oxygenase 2 Homo sapiens 27-31 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Heme 71-75 heme oxygenase 2 Homo sapiens 223-227 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Iron 76-80 heme oxygenase 2 Homo sapiens 44-48 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Iron 76-80 heme oxygenase 2 Homo sapiens 223-227 11554454-4 2001 We examined interaction of HO-2 HRMs with Fe-PP, Zn-protoporphyrin IX (Zn-PP; HO-2 inhibitor), and protoporphyrin IX (PP IX). zn-pp 71-76 heme oxygenase 2 Homo sapiens 27-31 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Cysteine 96-104 heme oxygenase 2 Homo sapiens 44-48 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Sulfhydryl Compounds 105-110 heme oxygenase 2 Homo sapiens 44-48 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Heme 71-75 heme oxygenase 2 Homo sapiens 44-48 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Heme 71-75 heme oxygenase 2 Homo sapiens 223-227 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Metalloporphyrins 250-267 heme oxygenase 2 Homo sapiens 44-48 11344084-1 2001 In this study we tested the hypothesis that expression of heme oxygenases HO-1 and HO-2, which are responsible for the production of carbon monoxide, are reduced in the placenta and placental bed of pregnancies complicated by preeclampsia (PE) and fetal growth restriction (FGR) compared with control third-trimester pregnancies. Carbon Monoxide 133-148 heme oxygenase 2 Homo sapiens 58-87 11502820-1 2001 Carbon monoxide, a gaseous activator of soluble guanylyl cyclase formed by a subtype of the enzyme heme oxygenase designated heme oxygenase-2 in vascular endothelium, has been found to dilate blood vessels independently from nitric oxide. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 125-141 11502820-4 2001 17beta-Estradiol, at a concentration such as that attained during the ovulatory phase of the menstrual cycle (10(-10) M), administrated for 4 h led to a 2-fold increase in intracellular carbon monoxide production and heme oxygenase-2 protein levels (P < 0.05). Estradiol 0-16 heme oxygenase 2 Homo sapiens 217-233 11502820-4 2001 17beta-Estradiol, at a concentration such as that attained during the ovulatory phase of the menstrual cycle (10(-10) M), administrated for 4 h led to a 2-fold increase in intracellular carbon monoxide production and heme oxygenase-2 protein levels (P < 0.05). Carbon Monoxide 186-201 heme oxygenase 2 Homo sapiens 217-233 23045070-2 2001 This unit describes protocols for assessing the expression and regulation of specific HO-1 and HO-2 mRNAs by in situ hybridization using digoxigenin-tagged probes. Digoxigenin 137-148 heme oxygenase 2 Homo sapiens 95-99 11235674-0 2001 [Radiolytic oxidation of tamoxifen with the free radicals OH- and/or HO2-]. Tamoxifen 25-34 heme oxygenase 2 Homo sapiens 69-72 11245628-6 2001 NO induction of HO-1 was not mediated via guanylyl cyclase and was not attenuated by 1 microM dexamethasone, although dexamethasone increased HO-2 protein. Dexamethasone 118-131 heme oxygenase 2 Homo sapiens 142-146 11235674-3 2001 We have investigated the ability of tamoxifen to scavenge, in vitro, *OH and (or) HO2* free radicals that are produced by water radiolysis. Tamoxifen 36-45 heme oxygenase 2 Homo sapiens 82-85 11235674-3 2001 We have investigated the ability of tamoxifen to scavenge, in vitro, *OH and (or) HO2* free radicals that are produced by water radiolysis. Water 122-127 heme oxygenase 2 Homo sapiens 82-85 11208917-14 2001 We hypothesize that HO-1 protects against further damage by contributing to controlled cell death through their intrinsic suicide program, while HO-2 is involved in suppression of inflammatory response by NO derived radicals. no derived radicals 205-224 heme oxygenase 2 Homo sapiens 145-149 11950143-12 2001 HO-2, which is the constitutive form, in addition to maintaining cell heme homeostasis, inactivates NO derived radicals. Heme 70-74 heme oxygenase 2 Homo sapiens 0-4 11950143-12 2001 HO-2, which is the constitutive form, in addition to maintaining cell heme homeostasis, inactivates NO derived radicals. no derived radicals 100-119 heme oxygenase 2 Homo sapiens 0-4 11093717-1 2000 Methanolysis of 2,4,6-tri-O-benzoyl-2,3-dibromo-3-deoxy-D-altrono-1,5-lactone gave methyl 3-bromo-3-deoxy-2,4,6-tri-O-benzoyl-alpha-D-ribo-hex-2-ulofuranosonat e (3) and the anomeric mixture of the analogous 4,6-di-O-benzoyl derivative, having HO-2 free. 2,4,6-tri-o-benzoyl-2,3-dibromo-3-deoxy-d-altrono-1,5-lactone 16-77 heme oxygenase 2 Homo sapiens 244-248 11093717-1 2000 Methanolysis of 2,4,6-tri-O-benzoyl-2,3-dibromo-3-deoxy-D-altrono-1,5-lactone gave methyl 3-bromo-3-deoxy-2,4,6-tri-O-benzoyl-alpha-D-ribo-hex-2-ulofuranosonat e (3) and the anomeric mixture of the analogous 4,6-di-O-benzoyl derivative, having HO-2 free. 3-bromo-3-deoxy-2,4,6-tri-o-benzoyl-alpha-d-ribo-hex-2-ulofuranosonat e 90-161 heme oxygenase 2 Homo sapiens 244-248 11093717-1 2000 Methanolysis of 2,4,6-tri-O-benzoyl-2,3-dibromo-3-deoxy-D-altrono-1,5-lactone gave methyl 3-bromo-3-deoxy-2,4,6-tri-O-benzoyl-alpha-D-ribo-hex-2-ulofuranosonat e (3) and the anomeric mixture of the analogous 4,6-di-O-benzoyl derivative, having HO-2 free. 4,6-di-o-benzoyl 208-224 heme oxygenase 2 Homo sapiens 244-248 10490932-10 1999 HO-2 antisense ODN inhibited heme-induced HO activity by 21%. Heme 29-33 heme oxygenase 2 Homo sapiens 0-4 10990066-1 2000 There is increasing evidence that the heme oxygenase-2 (HO-2)/carbon monoxide (CO) pathway and the nitric oxide synthase (NOS)/nitric oxide (NO) pathway functionally cross-talk. Carbon Monoxide 62-77 heme oxygenase 2 Homo sapiens 38-54 10990066-1 2000 There is increasing evidence that the heme oxygenase-2 (HO-2)/carbon monoxide (CO) pathway and the nitric oxide synthase (NOS)/nitric oxide (NO) pathway functionally cross-talk. Carbon Monoxide 62-77 heme oxygenase 2 Homo sapiens 56-60 10990066-1 2000 There is increasing evidence that the heme oxygenase-2 (HO-2)/carbon monoxide (CO) pathway and the nitric oxide synthase (NOS)/nitric oxide (NO) pathway functionally cross-talk. Carbon Monoxide 79-81 heme oxygenase 2 Homo sapiens 38-54 10990066-1 2000 There is increasing evidence that the heme oxygenase-2 (HO-2)/carbon monoxide (CO) pathway and the nitric oxide synthase (NOS)/nitric oxide (NO) pathway functionally cross-talk. Carbon Monoxide 79-81 heme oxygenase 2 Homo sapiens 56-60 10872744-4 2000 In a rather short span of the past 10 years following the discovery of high levels of a second form of the enzyme, HO-2, in the brain, suggesting that "heme oxygenase in the brain has functions aside from heme degradation" (Sun et al., 1990); concomitant with finding that another toxic gas, NO, is a signal molecule for generation of cGMP (Ignarro et al., 1982), the system was propelled into main stream research. Heme 152-156 heme oxygenase 2 Homo sapiens 115-119 10872744-4 2000 In a rather short span of the past 10 years following the discovery of high levels of a second form of the enzyme, HO-2, in the brain, suggesting that "heme oxygenase in the brain has functions aside from heme degradation" (Sun et al., 1990); concomitant with finding that another toxic gas, NO, is a signal molecule for generation of cGMP (Ignarro et al., 1982), the system was propelled into main stream research. Cyclic GMP 335-339 heme oxygenase 2 Homo sapiens 115-119 10766788-7 2000 Based on sequence identity with the mammalian enzymes the proximal ligand in HO-1 (His-25) and HO-2 (His-45) is conserved (His-20) in the bacterial enzyme. Histidine 83-86 heme oxygenase 2 Homo sapiens 95-99 10766788-7 2000 Based on sequence identity with the mammalian enzymes the proximal ligand in HO-1 (His-25) and HO-2 (His-45) is conserved (His-20) in the bacterial enzyme. Histidine 101-104 heme oxygenase 2 Homo sapiens 95-99 10766788-7 2000 Based on sequence identity with the mammalian enzymes the proximal ligand in HO-1 (His-25) and HO-2 (His-45) is conserved (His-20) in the bacterial enzyme. Histidine 101-104 heme oxygenase 2 Homo sapiens 95-99 10842752-2 2000 The HO-2 isoenzyme is predominantly a constitutive enzyme, which may serve to sequester heme as well as degrade it. Heme 88-92 heme oxygenase 2 Homo sapiens 4-8 10842752-6 2000 So far, HO-2 appears to be beneficial in oxygen toxicity in vivo, but the consequences of HO-2 overexpression have not yet been tested. Oxygen 41-47 heme oxygenase 2 Homo sapiens 8-12 10627295-1 2000 The purpose of this study was to examine the expression of hemeoxygenases HO-1 and HO-2, which are responsible for the production of carbon monoxide (CO), in the human placenta and placental bed and to determine the role of inhibitors of HO on placental perfusion pressure. Carbon Monoxide 133-148 heme oxygenase 2 Homo sapiens 59-87 10627295-1 2000 The purpose of this study was to examine the expression of hemeoxygenases HO-1 and HO-2, which are responsible for the production of carbon monoxide (CO), in the human placenta and placental bed and to determine the role of inhibitors of HO on placental perfusion pressure. Carbon Monoxide 150-152 heme oxygenase 2 Homo sapiens 59-87 10627295-6 2000 Within the placental bed, HO-2 was expressed by CTB in cell columns, the cytotrophoblast shell, and cell islands. ctb 48-51 heme oxygenase 2 Homo sapiens 26-30 10627295-7 2000 Both intravascular CTB and interstitial CTB expressed HO-2. ctb 19-22 heme oxygenase 2 Homo sapiens 54-58 10627295-7 2000 Both intravascular CTB and interstitial CTB expressed HO-2. ctb 40-43 heme oxygenase 2 Homo sapiens 54-58 10569611-1 1999 PURPOSE: The aim of present study was to determine the topographic relationship between heme oxygenase-2 (HO-2), which synthesizes carbon monoxide (CO), and neuronal nitric oxide synthase (nNOS), which generates nitric oxide (NO), in the autonomic nerves of the human ductus deferens and seminal vesicle. Carbon Monoxide 131-146 heme oxygenase 2 Homo sapiens 88-104 10569611-1 1999 PURPOSE: The aim of present study was to determine the topographic relationship between heme oxygenase-2 (HO-2), which synthesizes carbon monoxide (CO), and neuronal nitric oxide synthase (nNOS), which generates nitric oxide (NO), in the autonomic nerves of the human ductus deferens and seminal vesicle. Carbon Monoxide 131-146 heme oxygenase 2 Homo sapiens 106-110 10569611-1 1999 PURPOSE: The aim of present study was to determine the topographic relationship between heme oxygenase-2 (HO-2), which synthesizes carbon monoxide (CO), and neuronal nitric oxide synthase (nNOS), which generates nitric oxide (NO), in the autonomic nerves of the human ductus deferens and seminal vesicle. Carbon Monoxide 148-150 heme oxygenase 2 Homo sapiens 88-104 10569611-1 1999 PURPOSE: The aim of present study was to determine the topographic relationship between heme oxygenase-2 (HO-2), which synthesizes carbon monoxide (CO), and neuronal nitric oxide synthase (nNOS), which generates nitric oxide (NO), in the autonomic nerves of the human ductus deferens and seminal vesicle. Carbon Monoxide 148-150 heme oxygenase 2 Homo sapiens 106-110 10569611-1 1999 PURPOSE: The aim of present study was to determine the topographic relationship between heme oxygenase-2 (HO-2), which synthesizes carbon monoxide (CO), and neuronal nitric oxide synthase (nNOS), which generates nitric oxide (NO), in the autonomic nerves of the human ductus deferens and seminal vesicle. Nitric Oxide 166-178 heme oxygenase 2 Homo sapiens 88-104 10569611-1 1999 PURPOSE: The aim of present study was to determine the topographic relationship between heme oxygenase-2 (HO-2), which synthesizes carbon monoxide (CO), and neuronal nitric oxide synthase (nNOS), which generates nitric oxide (NO), in the autonomic nerves of the human ductus deferens and seminal vesicle. Nitric Oxide 166-178 heme oxygenase 2 Homo sapiens 106-110 10550617-3 1999 Because carbon monoxide (CO) is emerging as a putative mediator in the regulation of gastrointestinal motility, this study examined the presence of heme oxygenase (HO2), the constitutive form of the enzyme for CO production, in human stomach with particular attention to ICs. Carbon Monoxide 8-23 heme oxygenase 2 Homo sapiens 164-167 10550617-7 1999 The presence of HO2 in different cell types suggests that CO may serve as an intercellular messenger between myenteric neurons and ICs and between ICs and smooth muscle cells in human stomach. Carbon Monoxide 58-60 heme oxygenase 2 Homo sapiens 16-19 9618780-6 1998 Other potential novel pathways of LHRH release that are currently being explored include carbon monoxide generated by the action of heme oxygenase-2 on heme molecules and bradykinin acting via bradykinin B2 receptors. Carbon Monoxide 89-104 heme oxygenase 2 Homo sapiens 132-148 10491133-0 1999 Interaction of heme oxygenase-2 with nitric oxide donors. Nitric Oxide 37-49 heme oxygenase 2 Homo sapiens 15-31 10491133-4 1999 HO-2 is a hemoprotein and binds heme at heme regulatory motifs (HRMs) with a conserved Cys-Pro pair; two copies of HRM are present in HO-2 (Cys264 and Cys281). Heme 32-36 heme oxygenase 2 Homo sapiens 0-4 10491133-4 1999 HO-2 is a hemoprotein and binds heme at heme regulatory motifs (HRMs) with a conserved Cys-Pro pair; two copies of HRM are present in HO-2 (Cys264 and Cys281). Heme 40-44 heme oxygenase 2 Homo sapiens 0-4 10491133-4 1999 HO-2 is a hemoprotein and binds heme at heme regulatory motifs (HRMs) with a conserved Cys-Pro pair; two copies of HRM are present in HO-2 (Cys264 and Cys281). cysteinylproline 87-94 heme oxygenase 2 Homo sapiens 0-4 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. Nitroprusside 124-144 heme oxygenase 2 Homo sapiens 102-106 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. S-nitroglutathione 152-170 heme oxygenase 2 Homo sapiens 102-106 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. S-Nitrosoglutathione 172-176 heme oxygenase 2 Homo sapiens 102-106 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. S-Nitroso-N-Acetylpenicillamine 179-210 heme oxygenase 2 Homo sapiens 102-106 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. S-Nitroso-N-Acetylpenicillamine 212-216 heme oxygenase 2 Homo sapiens 102-106 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. linsidomine 221-244 heme oxygenase 2 Homo sapiens 102-106 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. Hydroxocobalamin 272-288 heme oxygenase 2 Homo sapiens 102-106 10491133-8 1999 A type II change (red shift) of the Soret band (405 nm --> 413-419 nm) was observed when wild-type HO-2 was treated with sodium nitroprusside (SNP), S-nitroglutathione (GSNO), S-nitroso-N-acetylpenicillamine (SNAP) or 3-morpholinosydnonimine (SIN-1); the NO scavenger, hydroxocobalamin (HCB) prevented the shift. Hydroxocobalamin 290-293 heme oxygenase 2 Homo sapiens 102-106 10491133-9 1999 Only SIN-1, which produces peroxynitrite by generating both NO and superoxide anion, decreased the Soret region absorption and the pyridine hemochromogen spectrum of HO-2; superoxide dismutase (SOD) blocked the decrease. pyridine 131-139 heme oxygenase 2 Homo sapiens 166-170 10491133-10 1999 Binding of heme to HO-2 protein was required for shift and/or decrease in absorption of the Soret band. Heme 11-15 heme oxygenase 2 Homo sapiens 19-23 10491133-12 1999 Again, trapping NO with HCB blocked HO-2 inactivation. Hydroxocobalamin 24-27 heme oxygenase 2 Homo sapiens 36-40 10491133-14 1999 CD data suggest that the decrease in HO-2 activity was not related to change by NO species of the secondary structure of HO-2. Cadmium 0-2 heme oxygenase 2 Homo sapiens 37-41 10491133-16 1999 The data are consistent with the possibility that NO interaction with HO-2-bound heme effects electronic interactions of residues involved in substrate binding and/or oxygen activation. Heme 81-85 heme oxygenase 2 Homo sapiens 70-74 10491133-16 1999 The data are consistent with the possibility that NO interaction with HO-2-bound heme effects electronic interactions of residues involved in substrate binding and/or oxygen activation. Oxygen 167-173 heme oxygenase 2 Homo sapiens 70-74 10491133-17 1999 The findings permit the hypothesis that HO-2 and NO are trans-inhibitors, whereby biological activity of NO is attenuated by interaction with HO-2, serving as an intracellular "sink" for the heme ligand, and NO inhibits HO-2 catalytic activity. Heme 191-195 heme oxygenase 2 Homo sapiens 40-44 10491133-17 1999 The findings permit the hypothesis that HO-2 and NO are trans-inhibitors, whereby biological activity of NO is attenuated by interaction with HO-2, serving as an intracellular "sink" for the heme ligand, and NO inhibits HO-2 catalytic activity. Heme 191-195 heme oxygenase 2 Homo sapiens 142-146 10491133-17 1999 The findings permit the hypothesis that HO-2 and NO are trans-inhibitors, whereby biological activity of NO is attenuated by interaction with HO-2, serving as an intracellular "sink" for the heme ligand, and NO inhibits HO-2 catalytic activity. Heme 191-195 heme oxygenase 2 Homo sapiens 142-146 9789638-1 1998 The most important steps of bilirubin metabolism involved in the pathophysiology of neonatal hyperbilirubinemia are: 1) hemoglobin degradation by heme oxygenase; 2) bilirubin binding to serum albumin; 3) bilirubin conjugation to acid glucoronic by glucoronyl transferase. Bilirubin 28-37 heme oxygenase 2 Homo sapiens 146-163 9789638-1 1998 The most important steps of bilirubin metabolism involved in the pathophysiology of neonatal hyperbilirubinemia are: 1) hemoglobin degradation by heme oxygenase; 2) bilirubin binding to serum albumin; 3) bilirubin conjugation to acid glucoronic by glucoronyl transferase. Bilirubin 98-107 heme oxygenase 2 Homo sapiens 146-163 9789638-1 1998 The most important steps of bilirubin metabolism involved in the pathophysiology of neonatal hyperbilirubinemia are: 1) hemoglobin degradation by heme oxygenase; 2) bilirubin binding to serum albumin; 3) bilirubin conjugation to acid glucoronic by glucoronyl transferase. Bilirubin 98-107 heme oxygenase 2 Homo sapiens 146-163 10487841-2 1999 Carbon monoxide (CO), produced by hemeoxygenases (HO-1 and HO-2), also activates soluble guanylate cyclase to increase cGMP. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 59-63 10487841-2 1999 Carbon monoxide (CO), produced by hemeoxygenases (HO-1 and HO-2), also activates soluble guanylate cyclase to increase cGMP. Carbon Monoxide 17-19 heme oxygenase 2 Homo sapiens 59-63 10487841-2 1999 Carbon monoxide (CO), produced by hemeoxygenases (HO-1 and HO-2), also activates soluble guanylate cyclase to increase cGMP. Cyclic GMP 119-123 heme oxygenase 2 Homo sapiens 59-63 10332482-10 1999 The dual expression of HO-2 with nNOS immunoreactivity in cell bodies and nerves suggests that there is an interaction between the CO and NO generating systems. Carbon Monoxide 131-133 heme oxygenase 2 Homo sapiens 23-27 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Carbon Monoxide 167-169 heme oxygenase 2 Homo sapiens 0-16 9468479-0 1998 Identification of histidine 45 as the axial heme iron ligand of heme oxygenase-2. Iron 49-53 heme oxygenase 2 Homo sapiens 64-80 9417019-2 1998 Comparison of the measured concentrations of OH and HO2 with calculations based on their production from water vapor, ozone, and methane demonstrate that these sources are insufficient to explain the observed radical concentrations in the upper troposphere. Water 106-111 heme oxygenase 2 Homo sapiens 53-56 9354392-2 1997 Treatment with each of three NO donors, sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione, caused noticeable increases in the expression levels of heme oxygenase- mRNA, but not heme oxygenase-2 mRNA. Nitroprusside 40-60 heme oxygenase 2 Homo sapiens 202-218 9354392-2 1997 Treatment with each of three NO donors, sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione, caused noticeable increases in the expression levels of heme oxygenase- mRNA, but not heme oxygenase-2 mRNA. linsidomine 62-85 heme oxygenase 2 Homo sapiens 202-218 9354392-2 1997 Treatment with each of three NO donors, sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione, caused noticeable increases in the expression levels of heme oxygenase- mRNA, but not heme oxygenase-2 mRNA. S-Nitrosoglutathione 91-114 heme oxygenase 2 Homo sapiens 202-218 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Heme 130-134 heme oxygenase 2 Homo sapiens 0-16 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Heme 130-134 heme oxygenase 2 Homo sapiens 18-22 9468479-0 1998 Identification of histidine 45 as the axial heme iron ligand of heme oxygenase-2. Histidine 18-27 heme oxygenase 2 Homo sapiens 64-80 9468479-0 1998 Identification of histidine 45 as the axial heme iron ligand of heme oxygenase-2. Heme 44-48 heme oxygenase 2 Homo sapiens 64-80 9468479-1 1998 A truncated, soluble, and enzymatically active form of human heme oxygenase-2 (DeltaHHO2) was expressed in Escherichia coli. deltahho2 79-88 heme oxygenase 2 Homo sapiens 61-77 9468479-2 1998 To identify the axial heme ligand of HO-2, His-45 to Ala (DeltaH45A) and His-152 to Ala (DeltaH152A) mutants have been prepared using this expression system. Heme 22-26 heme oxygenase 2 Homo sapiens 37-41 9457891-0 1998 Direct observation of HO2/O2- free radicals generated in water by a high-linear energy transfer pulsed heavy-ion beam. Water 57-62 heme oxygenase 2 Homo sapiens 22-25 9457891-1 1998 The formation and decay of HO2/O2- radical from the radiolysis of water by heavy 36S16+ ions (2.7 GeV) have been observed by time-resolved absorption spectroscopy at 260 nm. o2- radical 31-42 heme oxygenase 2 Homo sapiens 27-30 9457891-1 1998 The formation and decay of HO2/O2- radical from the radiolysis of water by heavy 36S16+ ions (2.7 GeV) have been observed by time-resolved absorption spectroscopy at 260 nm. Water 66-71 heme oxygenase 2 Homo sapiens 27-30 9457891-3 1998 In deaerated water, for a linear energy transfer (LET) of 250 eV/nm, the yield of HO2/O2- is (6 +/- 2) x 10(-9) mol J-1. Water 13-18 heme oxygenase 2 Homo sapiens 82-85 9457891-3 1998 In deaerated water, for a linear energy transfer (LET) of 250 eV/nm, the yield of HO2/O2- is (6 +/- 2) x 10(-9) mol J-1. o2- is 86-92 heme oxygenase 2 Homo sapiens 82-85 18259411-1 1997 High-frequency wavelength modulation spectroscopy (WMS) has been applied to the detection of the hydroperoxyl radical (HO2 ) in a laser photolysis and long-path absorption pump-probe kinetics reactor with a near-infrared distributed feedback diode laser. Hydroperoxy radical 97-117 heme oxygenase 2 Homo sapiens 119-122 18259411-2 1997 The HO2 is formed by the 355-nm photolysis of Cl2 in the presence of CH3 OH and O2 and monitored by a phase-sensitive detection of the second-harmonic (2f ) signal in the 2?1 band with a 1.5- ?m diode laser directly modulated at 5 MHz. Methanol 69-75 heme oxygenase 2 Homo sapiens 4-7 9254594-3 1997 The binding interactions of HO2--Co(III)-CodPEP (CodPEP) with CGTACG have been studied by 2D NMR and molecular modeling. cgtacg 62-68 heme oxygenase 2 Homo sapiens 28-31 9108252-4 1997 The structures of two green forms of cobalt-PEP species, HO2-Co(III)-PEP (denoted CoPEP) and deglycosylated HO2-Co(III)-PEP (denoted CodPEP) have been obtained by NOE restrained refinements. Cobalt 37-43 heme oxygenase 2 Homo sapiens 57-60 9108252-5 1997 Earlier studies of the related HO2-Co(III)-BLM A2 proposed that two chiral conformers (form A or B) could exist with either the beta-aminoalanine primary amine (A,NH2) or the mannose carbamoyl nitrogen (M,NH2) as the axial ligand. beta-aminoalanine primary amine 128-159 heme oxygenase 2 Homo sapiens 31-34 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Biliverdine 146-165 heme oxygenase 2 Homo sapiens 0-16 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Biliverdine 146-165 heme oxygenase 2 Homo sapiens 18-22 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Carbon Monoxide 167-169 heme oxygenase 2 Homo sapiens 18-22 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Iron 174-176 heme oxygenase 2 Homo sapiens 0-16 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Iron 174-176 heme oxygenase 2 Homo sapiens 18-22 9116047-5 1997 The HO-2 GRE was tested for responsiveness to dexamethasone (DX) using both a promoterless CAT expression vector, and a heterologous promoter containing luciferase expression vector in HeLa cells. Dexamethasone 46-59 heme oxygenase 2 Homo sapiens 4-8 9116047-10 1997 The increase in the HO-2 transcript was accompanied by an increase in HO-2 protein, as assessed by Western blot analysis, and an increase in HO activity, as measured by bilirubin formation. Bilirubin 169-178 heme oxygenase 2 Homo sapiens 20-24 8764571-4 1996 In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs. Nitroprusside 89-109 heme oxygenase 2 Homo sapiens 259-275 8764571-4 1996 In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs. linsidomine 111-134 heme oxygenase 2 Homo sapiens 259-275 8764571-4 1996 In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs. S-Nitrosoglutathione 140-163 heme oxygenase 2 Homo sapiens 259-275 8742445-1 1995 HAEM oxygenase-2 (HO-2) is the neuronal isoform of the only known mammalian enzyme generating the new transmitter candidate, carbon monoxide. Carbon Monoxide 125-140 heme oxygenase 2 Homo sapiens 0-16 8570637-1 1996 Heme oxygenase 2 (HO-2), which synthesizes carbon monoxide (CO), has been localized by immunohistochemistry to endothelial cells and adventitial nerves of blood vessels. Carbon Monoxide 43-58 heme oxygenase 2 Homo sapiens 0-16 8570637-1 1996 Heme oxygenase 2 (HO-2), which synthesizes carbon monoxide (CO), has been localized by immunohistochemistry to endothelial cells and adventitial nerves of blood vessels. Carbon Monoxide 43-58 heme oxygenase 2 Homo sapiens 18-22 8570637-1 1996 Heme oxygenase 2 (HO-2), which synthesizes carbon monoxide (CO), has been localized by immunohistochemistry to endothelial cells and adventitial nerves of blood vessels. Carbon Monoxide 60-62 heme oxygenase 2 Homo sapiens 0-16 8570637-1 1996 Heme oxygenase 2 (HO-2), which synthesizes carbon monoxide (CO), has been localized by immunohistochemistry to endothelial cells and adventitial nerves of blood vessels. Carbon Monoxide 60-62 heme oxygenase 2 Homo sapiens 18-22 8742445-1 1995 HAEM oxygenase-2 (HO-2) is the neuronal isoform of the only known mammalian enzyme generating the new transmitter candidate, carbon monoxide. Carbon Monoxide 125-140 heme oxygenase 2 Homo sapiens 18-22 11539176-3 1994 Good agreement between models and observations of CO, O2, O3, and the escape flux of atomic hydrogen can be achieved, using only gas-phase chemistry, by varying the recommended rate constants for the reactions CO + OH and OH + HO2 within their specified uncertainties. Carbon Monoxide 50-52 heme oxygenase 2 Homo sapiens 227-230 7890772-1 1995 Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. Heme 18-22 heme oxygenase 2 Homo sapiens 85-101 7890772-6 1995 EPR and Raman scattering studies indicated that a neutral imidazole of a histidine residue served as the proximal ligand in the heme-heme oxygenase-2 fragment complex. imidazole 58-67 heme oxygenase 2 Homo sapiens 133-149 7890772-6 1995 EPR and Raman scattering studies indicated that a neutral imidazole of a histidine residue served as the proximal ligand in the heme-heme oxygenase-2 fragment complex. Histidine 73-82 heme oxygenase 2 Homo sapiens 133-149 7890772-7 1995 The reaction with hydrogen peroxide converted the heme of the heme oxygenase-2 fragment complex into a verdoheme-like intermediate, while the reaction with m-chloroperbenzoic acid yielded a oxoferryl species. Hydrogen Peroxide 18-35 heme oxygenase 2 Homo sapiens 62-78 7890772-7 1995 The reaction with hydrogen peroxide converted the heme of the heme oxygenase-2 fragment complex into a verdoheme-like intermediate, while the reaction with m-chloroperbenzoic acid yielded a oxoferryl species. Heme 50-54 heme oxygenase 2 Homo sapiens 62-78 7890772-7 1995 The reaction with hydrogen peroxide converted the heme of the heme oxygenase-2 fragment complex into a verdoheme-like intermediate, while the reaction with m-chloroperbenzoic acid yielded a oxoferryl species. verdoheme 103-112 heme oxygenase 2 Homo sapiens 62-78 7890772-7 1995 The reaction with hydrogen peroxide converted the heme of the heme oxygenase-2 fragment complex into a verdoheme-like intermediate, while the reaction with m-chloroperbenzoic acid yielded a oxoferryl species. oxoferryl 190-199 heme oxygenase 2 Homo sapiens 62-78 7705297-3 1994 Oxidase-catalyzed univalent reduction of O2 (S = 1; triplet multiplicity) yields hydrodioxylic acid (HO2) and its conjugate base superoxide, O2- (S = 1/2; doublet multiplicity). Oxygen 41-43 heme oxygenase 2 Homo sapiens 101-104 7705297-3 1994 Oxidase-catalyzed univalent reduction of O2 (S = 1; triplet multiplicity) yields hydrodioxylic acid (HO2) and its conjugate base superoxide, O2- (S = 1/2; doublet multiplicity). hydrodioxylic acid 81-99 heme oxygenase 2 Homo sapiens 101-104 7705297-3 1994 Oxidase-catalyzed univalent reduction of O2 (S = 1; triplet multiplicity) yields hydrodioxylic acid (HO2) and its conjugate base superoxide, O2- (S = 1/2; doublet multiplicity). Superoxides 129-139 heme oxygenase 2 Homo sapiens 101-104 7525927-2 1994 Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin. Carbon Monoxide 179-194 heme oxygenase 2 Homo sapiens 47-51 7525927-2 1994 Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin. Bilirubin 217-226 heme oxygenase 2 Homo sapiens 47-51 7929359-0 1994 Interaction of Fe-protoporphyrin IX and heme analogues with purified recombinant heme oxygenase-2, the constitutive isozyme of the brain and testes. ferriheme b(1-) 15-35 heme oxygenase 2 Homo sapiens 81-97 7929359-0 1994 Interaction of Fe-protoporphyrin IX and heme analogues with purified recombinant heme oxygenase-2, the constitutive isozyme of the brain and testes. Heme 40-44 heme oxygenase 2 Homo sapiens 81-97 7929359-7 1994 A multistep protocol developed for isolation of HO-2 resulted in a homogeneous protein with a specific activity up to 6,500 nmol of bilirubin/mg/h. Bilirubin 132-141 heme oxygenase 2 Homo sapiens 48-52 7929359-9 1994 HO-2 binds Fe-protoporphyrin (heme) at near molar unity to give a complex with the absorption maximum at 403 nm. fe-protoporphyrin 11-28 heme oxygenase 2 Homo sapiens 0-4 7929359-9 1994 HO-2 binds Fe-protoporphyrin (heme) at near molar unity to give a complex with the absorption maximum at 403 nm. Heme 30-34 heme oxygenase 2 Homo sapiens 0-4 7929359-11 1994 The Soret band of the CO complex of ferrous heme.HO-2 is at 420 nm, and alpha and beta bands are at 540 and 572 nm, respectively. ferrous heme 36-48 heme oxygenase 2 Homo sapiens 49-53 7929359-14 1994 When HO-2 was preincubated (10 min at 4 degrees C) with Fe-protoporphyrin, the cobalt complex did not inhibit enzyme activity, whereas the Zn-protoporphyrin effectively inhibited activity. fe-protoporphyrin 56-73 heme oxygenase 2 Homo sapiens 5-9 7929359-14 1994 When HO-2 was preincubated (10 min at 4 degrees C) with Fe-protoporphyrin, the cobalt complex did not inhibit enzyme activity, whereas the Zn-protoporphyrin effectively inhibited activity. Cobalt 79-85 heme oxygenase 2 Homo sapiens 5-9 7929359-14 1994 When HO-2 was preincubated (10 min at 4 degrees C) with Fe-protoporphyrin, the cobalt complex did not inhibit enzyme activity, whereas the Zn-protoporphyrin effectively inhibited activity. zn-protoporphyrin 139-156 heme oxygenase 2 Homo sapiens 5-9 7929359-15 1994 Calorimetric measurements suggest that HO-2/heme interaction involves one type of association producing a single heat absorption peak upon melting of the complex and that the unfolding is not reversible. Heme 44-48 heme oxygenase 2 Homo sapiens 39-43 11539176-3 1994 Good agreement between models and observations of CO, O2, O3, and the escape flux of atomic hydrogen can be achieved, using only gas-phase chemistry, by varying the recommended rate constants for the reactions CO + OH and OH + HO2 within their specified uncertainties. Hydrogen 92-100 heme oxygenase 2 Homo sapiens 227-230 7508261-1 1994 The oxidation of Co(II) bleomycin A2 by dioxygen leads to two products, HO2-Co(III) bleomycin A2 (form I) and Co(III) bleomycin A2 (form II). co(ii) bleomycin 17-33 heme oxygenase 2 Homo sapiens 72-75 7508261-1 1994 The oxidation of Co(II) bleomycin A2 by dioxygen leads to two products, HO2-Co(III) bleomycin A2 (form I) and Co(III) bleomycin A2 (form II). co(iii) bleomycin a2 76-96 heme oxygenase 2 Homo sapiens 72-75 1334801-4 1992 The results show that HO-2 and HO-3 of Ins(1,4,5)P3 have a relatively insignificant role in receptor binding and calcium release. Inositol 1,4,5-Trisphosphate 39-51 heme oxygenase 2 Homo sapiens 22-35 8455037-1 1993 In mammalian systems, the heme oxygenase (HO) isozymes HO-1 (HSP32) and HO-2 oxidatively cleave the heme molecule to produce bile pigments and carbon monoxide. Heme 26-30 heme oxygenase 2 Homo sapiens 72-76 8455037-1 1993 In mammalian systems, the heme oxygenase (HO) isozymes HO-1 (HSP32) and HO-2 oxidatively cleave the heme molecule to produce bile pigments and carbon monoxide. Carbon Monoxide 143-158 heme oxygenase 2 Homo sapiens 72-76 1810305-3 1991 An analogous substitution pattern was observed for HO-2 and -3 of a simpler idopyranose unit, in the sulfation of methyl 4,6-O-benzylidene-alpha-D-idopyranoside (12). idose 76-87 heme oxygenase 2 Homo sapiens 51-62 1396715-7 1992 With respect to the galactose moiety, it is shown here that HO-3" and HO-2" are necessary for hydrolysis of the substrates by lactase. Galactose 20-29 heme oxygenase 2 Homo sapiens 70-74 1810305-3 1991 An analogous substitution pattern was observed for HO-2 and -3 of a simpler idopyranose unit, in the sulfation of methyl 4,6-O-benzylidene-alpha-D-idopyranoside (12). methyl 4,6-O-benzylidene-idopyranoside 114-160 heme oxygenase 2 Homo sapiens 51-62 1810305-5 1991 It is attributed to a difference between the two polymers in the relative orientation of their neighboring amino sugar residues, whereby there is an unobstructed access of the reagent in one instance, and hindrance of HO-2 selectively in the other. Polymers 49-57 heme oxygenase 2 Homo sapiens 218-222 1810305-5 1991 It is attributed to a difference between the two polymers in the relative orientation of their neighboring amino sugar residues, whereby there is an unobstructed access of the reagent in one instance, and hindrance of HO-2 selectively in the other. Amino Sugars 107-118 heme oxygenase 2 Homo sapiens 218-222 32891045-7 2020 The seasonal variation in Delta17O(NO3-) indicates the relative importance of O3 and HO2/RO2/OH in NOx oxidation processes among different seasons. Ozone 36-38 heme oxygenase 2 Homo sapiens 85-88 1667772-3 1991 ), directly or via HO2., produces the chlorophyll enolate-ion (Molish"s intermediate) that is oxidized to Mg-chlorine(s). chlorophyll enolate 38-57 heme oxygenase 2 Homo sapiens 19-22 1667772-3 1991 ), directly or via HO2., produces the chlorophyll enolate-ion (Molish"s intermediate) that is oxidized to Mg-chlorine(s). mg-chlorine 106-117 heme oxygenase 2 Homo sapiens 19-22 1965680-1 1990 The rate of interaction between H2O2 and the DNA-Cu(I) complex increases with pH and with salt (NaCl) concentration, suggesting that HO2- is involved. Hydrogen Peroxide 32-36 heme oxygenase 2 Homo sapiens 133-136 1965680-1 1990 The rate of interaction between H2O2 and the DNA-Cu(I) complex increases with pH and with salt (NaCl) concentration, suggesting that HO2- is involved. Salts 90-94 heme oxygenase 2 Homo sapiens 133-136 1965680-1 1990 The rate of interaction between H2O2 and the DNA-Cu(I) complex increases with pH and with salt (NaCl) concentration, suggesting that HO2- is involved. Sodium Chloride 96-100 heme oxygenase 2 Homo sapiens 133-136 1965680-2 1990 The pH dependence can be fitted, assuming k(DNA-Cu(I) + H2O2) = 1 M-1 S-1 and k(DNA-Cu(I) + HO2-) = 10(5) M-1 S-1 (at low salt concentrations). Salts 122-126 heme oxygenase 2 Homo sapiens 92-95 33803289-7 2021 The DMF treatment was associated with no changes in virus replication; higher expressions of the antioxidant enzymes NQO1, GPX1, and HO-1 in the brain and PRDX1 and HO-2 in the spleen; lower levels of 8-OHdG and 3NT; a lower optical redox ratio. Dimethyl Fumarate 4-7 heme oxygenase 2 Homo sapiens 165-169 34973332-0 2022 Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells. ferric heme 49-60 heme oxygenase 2 Homo sapiens 0-16 34656601-7 2022 In gas phase, self-cyclization of alkoxy radical (RO ) leads to formation of HO2 and highly-oxygenated molecules, which cause formation of secondary organic aerosol. alkoxy radical 34-48 heme oxygenase 2 Homo sapiens 78-81 33591185-1 2021 In addition to its vital significance in combustion and atmospheric chemistry, the reaction between H" and HO2 on the ground triplet state represents a prototype with multiple product channels, including H2 + O2, OH + OH, O + H2O, and H + H"O2. Water 226-229 heme oxygenase 2 Homo sapiens 107-110 34673391-3 2022 Intriguingly, the analytical results for degradation intermediates and other characterization techniques demonstrate that the pollutants adsorbed on the graphitized C of BiOBr-Cg can be directly excited through light irradiation and react along the organic radical degradation pathway in addition to pollutant degradation by holes and HO2 /O2 -. biobr-cg 170-178 heme oxygenase 2 Homo sapiens 335-338 34673391-3 2022 Intriguingly, the analytical results for degradation intermediates and other characterization techniques demonstrate that the pollutants adsorbed on the graphitized C of BiOBr-Cg can be directly excited through light irradiation and react along the organic radical degradation pathway in addition to pollutant degradation by holes and HO2 /O2 -. Oxygen 340-344 heme oxygenase 2 Homo sapiens 335-338 34973332-0 2022 Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells. ferric heme 49-60 heme oxygenase 2 Homo sapiens 18-22 34973332-3 2022 While much is known about the regulation and physiological function of HO-1, comparatively little is known about the role of HO-2 in regulating heme homeostasis. Heme 144-148 heme oxygenase 2 Homo sapiens 125-129 34973332-4 2022 The biochemical necessity for expressing constitutive HO-2 is largely dependent on whether heme is sufficiently abundant and accessible as a substrate under conditions in which HO-1 is not induced. Heme 91-95 heme oxygenase 2 Homo sapiens 54-58 34973332-5 2022 By measuring labile heme, total heme, and bilirubin in human embryonic kidney HEK293 cells with silenced or over-expressed HO-2, as well as various HO-2 mutant alleles, we found that endogenous heme is too limiting a substrate to observe HO-2-dependent heme degradation. Heme 20-24 heme oxygenase 2 Homo sapiens 238-242 34973332-5 2022 By measuring labile heme, total heme, and bilirubin in human embryonic kidney HEK293 cells with silenced or over-expressed HO-2, as well as various HO-2 mutant alleles, we found that endogenous heme is too limiting a substrate to observe HO-2-dependent heme degradation. Heme 32-36 heme oxygenase 2 Homo sapiens 238-242 34973332-5 2022 By measuring labile heme, total heme, and bilirubin in human embryonic kidney HEK293 cells with silenced or over-expressed HO-2, as well as various HO-2 mutant alleles, we found that endogenous heme is too limiting a substrate to observe HO-2-dependent heme degradation. Bilirubin 42-51 heme oxygenase 2 Homo sapiens 238-242 34973332-5 2022 By measuring labile heme, total heme, and bilirubin in human embryonic kidney HEK293 cells with silenced or over-expressed HO-2, as well as various HO-2 mutant alleles, we found that endogenous heme is too limiting a substrate to observe HO-2-dependent heme degradation. Heme 253-257 heme oxygenase 2 Homo sapiens 238-242 34973332-6 2022 Rather, we discovered a novel role for HO-2 in the binding and buffering of heme. Heme 76-80 heme oxygenase 2 Homo sapiens 39-43 34973332-7 2022 Taken together, in the absence of excess heme, we propose that HO-2 regulates heme homeostasis by acting as a heme buffering factor that controls heme bioavailability. Heme 78-82 heme oxygenase 2 Homo sapiens 63-67 34973332-7 2022 Taken together, in the absence of excess heme, we propose that HO-2 regulates heme homeostasis by acting as a heme buffering factor that controls heme bioavailability. Heme 110-114 heme oxygenase 2 Homo sapiens 63-67 34973332-7 2022 Taken together, in the absence of excess heme, we propose that HO-2 regulates heme homeostasis by acting as a heme buffering factor that controls heme bioavailability. Heme 146-150 heme oxygenase 2 Homo sapiens 63-67 34973332-8 2022 When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation. Heme 5-9 heme oxygenase 2 Homo sapiens 49-53 34973332-8 2022 When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation. Heme 91-95 heme oxygenase 2 Homo sapiens 49-53 34973332-10 2022 Moreover, the change in bioavailable heme due to HO-2 overexpression, which selectively binds ferric over ferrous heme, is consistent with the labile heme pool being oxidized, thereby providing new insights into heme trafficking and signaling. Heme 37-41 heme oxygenase 2 Homo sapiens 49-53 34973332-10 2022 Moreover, the change in bioavailable heme due to HO-2 overexpression, which selectively binds ferric over ferrous heme, is consistent with the labile heme pool being oxidized, thereby providing new insights into heme trafficking and signaling. Ferric enterobactin ion 94-100 heme oxygenase 2 Homo sapiens 49-53 34973332-10 2022 Moreover, the change in bioavailable heme due to HO-2 overexpression, which selectively binds ferric over ferrous heme, is consistent with the labile heme pool being oxidized, thereby providing new insights into heme trafficking and signaling. ferrous heme 106-118 heme oxygenase 2 Homo sapiens 49-53 34973332-10 2022 Moreover, the change in bioavailable heme due to HO-2 overexpression, which selectively binds ferric over ferrous heme, is consistent with the labile heme pool being oxidized, thereby providing new insights into heme trafficking and signaling. Heme 150-154 heme oxygenase 2 Homo sapiens 49-53 34973332-10 2022 Moreover, the change in bioavailable heme due to HO-2 overexpression, which selectively binds ferric over ferrous heme, is consistent with the labile heme pool being oxidized, thereby providing new insights into heme trafficking and signaling. Heme 212-216 heme oxygenase 2 Homo sapiens 49-53 34438153-3 2021 In this work, we comprehensively investigated the reaction mechanism of isoprene with Cl using quantum chemistry calculation, and first elaborated the specific reaction mechanisms of chloroalkenyl peroxy radicals with HO2/NO and the formation of 2-methylbut-3-enal, highlighting their important roles in the SOA formation. isoprene 72-80 heme oxygenase 2 Homo sapiens 218-224 34438153-3 2021 In this work, we comprehensively investigated the reaction mechanism of isoprene with Cl using quantum chemistry calculation, and first elaborated the specific reaction mechanisms of chloroalkenyl peroxy radicals with HO2/NO and the formation of 2-methylbut-3-enal, highlighting their important roles in the SOA formation. chloroalkenyl peroxy radicals 183-212 heme oxygenase 2 Homo sapiens 218-224 34438153-3 2021 In this work, we comprehensively investigated the reaction mechanism of isoprene with Cl using quantum chemistry calculation, and first elaborated the specific reaction mechanisms of chloroalkenyl peroxy radicals with HO2/NO and the formation of 2-methylbut-3-enal, highlighting their important roles in the SOA formation. 2-Methyl-3-butenal 246-264 heme oxygenase 2 Homo sapiens 218-224 34618435-5 2021 Radical-terminating hydroperoxide formation from the peroxy radical (RO2) reaction with HO2 and organonitrate formation from RO2 + NO are not observed in the gas phase, possibly due to low volatility; constraints for their branching ratios are instead derived by mass balance. Hydrogen Peroxide 20-33 heme oxygenase 2 Homo sapiens 88-91 34618435-5 2021 Radical-terminating hydroperoxide formation from the peroxy radical (RO2) reaction with HO2 and organonitrate formation from RO2 + NO are not observed in the gas phase, possibly due to low volatility; constraints for their branching ratios are instead derived by mass balance. Oxygen 53-67 heme oxygenase 2 Homo sapiens 88-91 34618435-5 2021 Radical-terminating hydroperoxide formation from the peroxy radical (RO2) reaction with HO2 and organonitrate formation from RO2 + NO are not observed in the gas phase, possibly due to low volatility; constraints for their branching ratios are instead derived by mass balance. ro2 69-72 heme oxygenase 2 Homo sapiens 88-91 35533403-5 2022 Then, further transformation could not be induced from the addition of HO2- and CH3OO- to p-BQ. quinone 90-94 heme oxygenase 2 Homo sapiens 71-74 34494036-7 2021 According to the ME simulations, without any adjustment to energies, the most important and second most important product channels at the high temperatures are isoprene + HO2 (yield > 91%) and (2R/S)-3-methyl-1,2-epoxybut-3-ene + OH (yield < 8%). isoprene 160-168 heme oxygenase 2 Homo sapiens 171-174 34691692-6 2021 The halogen atoms increased the abundance of "conventional" tropospheric oxidants (OH, HO2 and RO2) by 26%-73%, and enhanced oxidation of hydrocarbon by nearly a factor of two and the net ozone production by 55%. Halogens 4-11 heme oxygenase 2 Homo sapiens 87-90 35460631-1 2022 Carbon monoxide (CO), a member of the multifunctional gasotransmitters family produced by heme oxygenases (i.e., HO-1 and HO-2), has received significant attention because of its involvement in carbohydrate metabolism. Carbon Monoxide 0-15 heme oxygenase 2 Homo sapiens 122-126 35460631-1 2022 Carbon monoxide (CO), a member of the multifunctional gasotransmitters family produced by heme oxygenases (i.e., HO-1 and HO-2), has received significant attention because of its involvement in carbohydrate metabolism. Carbon Monoxide 17-19 heme oxygenase 2 Homo sapiens 122-126 35460631-1 2022 Carbon monoxide (CO), a member of the multifunctional gasotransmitters family produced by heme oxygenases (i.e., HO-1 and HO-2), has received significant attention because of its involvement in carbohydrate metabolism. Carbohydrates 194-206 heme oxygenase 2 Homo sapiens 122-126 35502893-4 2022 Mn(II) accelerates Fe(III) reduction, superoxide radical (HO2 /O2 -) formation, and hydroxyl radical (HO ) formation. Manganese(2+) 0-6 heme oxygenase 2 Homo sapiens 58-61 35502893-8 2022 The resulting binuclear complex undergoes intramolecular electron transfer to give Fe(II), which later generates HO from H2O2, plus MnO2+, which later decomposes to HO2 /O2 - (an Fe(III) reductant) and Mn(II), completing the catalytic cycle. ammonium ferrous sulfate 83-89 heme oxygenase 2 Homo sapiens 166-169 35502893-8 2022 The resulting binuclear complex undergoes intramolecular electron transfer to give Fe(II), which later generates HO from H2O2, plus MnO2+, which later decomposes to HO2 /O2 - (an Fe(III) reductant) and Mn(II), completing the catalytic cycle. Hydroxyl Radical 113-115 heme oxygenase 2 Homo sapiens 166-169 35502893-8 2022 The resulting binuclear complex undergoes intramolecular electron transfer to give Fe(II), which later generates HO from H2O2, plus MnO2+, which later decomposes to HO2 /O2 - (an Fe(III) reductant) and Mn(II), completing the catalytic cycle. Hydrogen Peroxide 122-126 heme oxygenase 2 Homo sapiens 166-169 35502893-8 2022 The resulting binuclear complex undergoes intramolecular electron transfer to give Fe(II), which later generates HO from H2O2, plus MnO2+, which later decomposes to HO2 /O2 - (an Fe(III) reductant) and Mn(II), completing the catalytic cycle. mno2+ 133-138 heme oxygenase 2 Homo sapiens 166-169 35502893-8 2022 The resulting binuclear complex undergoes intramolecular electron transfer to give Fe(II), which later generates HO from H2O2, plus MnO2+, which later decomposes to HO2 /O2 - (an Fe(III) reductant) and Mn(II), completing the catalytic cycle. Oxygen 171-175 heme oxygenase 2 Homo sapiens 166-169 35502893-8 2022 The resulting binuclear complex undergoes intramolecular electron transfer to give Fe(II), which later generates HO from H2O2, plus MnO2+, which later decomposes to HO2 /O2 - (an Fe(III) reductant) and Mn(II), completing the catalytic cycle. ferric sulfate 180-187 heme oxygenase 2 Homo sapiens 166-169 35502893-8 2022 The resulting binuclear complex undergoes intramolecular electron transfer to give Fe(II), which later generates HO from H2O2, plus MnO2+, which later decomposes to HO2 /O2 - (an Fe(III) reductant) and Mn(II), completing the catalytic cycle. Manganese(2+) 203-209 heme oxygenase 2 Homo sapiens 166-169 34517731-3 2022 We center our discussion on two HRM-containing proteins: human heme oxygenase-2, a protein that binds and degrades heme (releasing Fe2+ and CO) in its catalytic core and binds Fe3+-heme at HRMs located within an unstructured region of the enzyme, and the transcriptional regulator Rev-erbbeta, a protein that binds Fe3+-heme at an HRM and is involved in CO sensing. Heme 115-119 heme oxygenase 2 Homo sapiens 63-79 34517731-3 2022 We center our discussion on two HRM-containing proteins: human heme oxygenase-2, a protein that binds and degrades heme (releasing Fe2+ and CO) in its catalytic core and binds Fe3+-heme at HRMs located within an unstructured region of the enzyme, and the transcriptional regulator Rev-erbbeta, a protein that binds Fe3+-heme at an HRM and is involved in CO sensing. ammonium ferrous sulfate 131-135 heme oxygenase 2 Homo sapiens 63-79 34517731-3 2022 We center our discussion on two HRM-containing proteins: human heme oxygenase-2, a protein that binds and degrades heme (releasing Fe2+ and CO) in its catalytic core and binds Fe3+-heme at HRMs located within an unstructured region of the enzyme, and the transcriptional regulator Rev-erbbeta, a protein that binds Fe3+-heme at an HRM and is involved in CO sensing. Carbon Monoxide 140-142 heme oxygenase 2 Homo sapiens 63-79 34517731-3 2022 We center our discussion on two HRM-containing proteins: human heme oxygenase-2, a protein that binds and degrades heme (releasing Fe2+ and CO) in its catalytic core and binds Fe3+-heme at HRMs located within an unstructured region of the enzyme, and the transcriptional regulator Rev-erbbeta, a protein that binds Fe3+-heme at an HRM and is involved in CO sensing. ferric sulfate 176-180 heme oxygenase 2 Homo sapiens 63-79 34517731-3 2022 We center our discussion on two HRM-containing proteins: human heme oxygenase-2, a protein that binds and degrades heme (releasing Fe2+ and CO) in its catalytic core and binds Fe3+-heme at HRMs located within an unstructured region of the enzyme, and the transcriptional regulator Rev-erbbeta, a protein that binds Fe3+-heme at an HRM and is involved in CO sensing. Heme 181-185 heme oxygenase 2 Homo sapiens 63-79 34246992-5 2021 This is due to the formation of Cl2 - in seawater which could react with HO2 and prevent the formation of O2 -, thus inhibit the photo aging process of PP MPs under light irradiation. Oxygen 107-111 heme oxygenase 2 Homo sapiens 73-76 34255503-7 2021 Afternoon plumes displayed a rapid transition from VOC-sensitive to NOx-sensitive chemistry, driven by HOx (=OH + HO2) production from photolysis of nitrous acid (HONO) (48 +- 20% of primary HOx) and formaldehyde (HCHO) (26 +- 9%) emitted directly from the fire. Nitrous Acid 149-161 heme oxygenase 2 Homo sapiens 114-117 34255503-7 2021 Afternoon plumes displayed a rapid transition from VOC-sensitive to NOx-sensitive chemistry, driven by HOx (=OH + HO2) production from photolysis of nitrous acid (HONO) (48 +- 20% of primary HOx) and formaldehyde (HCHO) (26 +- 9%) emitted directly from the fire. Nitrous Acid 163-167 heme oxygenase 2 Homo sapiens 114-117 34213330-2 2021 The H-abstraction reactions from 3-pentanol by H, CH3, HO2, and OH radicals are significant in the 3-pentanol oxidation process. 3-PENTANOL 33-43 heme oxygenase 2 Homo sapiens 55-58 34213330-2 2021 The H-abstraction reactions from 3-pentanol by H, CH3, HO2, and OH radicals are significant in the 3-pentanol oxidation process. 3-PENTANOL 99-109 heme oxygenase 2 Homo sapiens 55-58 34213330-11 2021 The rate constants for the above H-abstraction reactions in the Carbonnier model were updated with the calculated results, followed by a modification based on the computed results of 3-pentanol + HO2 to obtain the revised model. 3-PENTANOL 183-193 heme oxygenase 2 Homo sapiens 196-199 34560924-0 2021 Upregulation of hemeoxygenase enzymes HO-1 and HO-2 following ischemia-reperfusion injury in connection with experimental cardiac arrest and cardiopulmonary resuscitation: Neuroprotective effects of methylene blue. Methylene Blue 199-213 heme oxygenase 2 Homo sapiens 47-51 34560924-9 2021 Our observations are the first to show that cardiac arrest followed by successful cardiopulmonary resuscitation results in significant alteration in cerebral concentrations of HO-1 and HO-2 levels indicating a prominent role of CO in brain pathology and methylene blue during CPR followed by induced hypothermia leading to superior neuroprotection after return of spontaneous circulation (ROSC), not reported earlier. Methylene Blue 254-268 heme oxygenase 2 Homo sapiens 185-189 35588835-5 2022 The lower delta18O-NO3- values (less than 52%) indicated the importance of peroxy radicals (RO2 or HO2) in NOx oxidation to NO3- formation pathways. peroxy radicals 75-90 heme oxygenase 2 Homo sapiens 99-102 35588835-6 2022 By the Monte Carlo simulation of delta18O-NO3- values of typhoons, the calculated oxidation proportions of NO by RO2 (or HO2) during the OH pathway ranged from 0% to 27% of In-fa and from 0% to 32% of Chanthu, respectively, in the three cities. in-fa 174-179 heme oxygenase 2 Homo sapiens 121-124 35182648-6 2022 HONO photolysis was a significant source of reactive radicals (ROx = OH + HO2 + RO2) in these air masses. Nitrous Acid 0-4 heme oxygenase 2 Homo sapiens 74-77 35182648-6 2022 HONO photolysis was a significant source of reactive radicals (ROx = OH + HO2 + RO2) in these air masses. reactive radicals 44-61 heme oxygenase 2 Homo sapiens 74-77 35182648-6 2022 HONO photolysis was a significant source of reactive radicals (ROx = OH + HO2 + RO2) in these air masses. ROX 63-66 heme oxygenase 2 Homo sapiens 74-77 35628518-8 2022 Moreover, our results suggest a potential role of HO-2 in erastin-induced ferroptosis. erastin 58-65 heme oxygenase 2 Homo sapiens 50-54 35533403-4 2022 For p-BQ, the nucleophilic attack of HO2-, CH3OO-, PMS, and PAA might prefer to occur on the carbonyl carbons, which have more positive atomic charges. quinone 4-8 heme oxygenase 2 Homo sapiens 37-40 35533403-4 2022 For p-BQ, the nucleophilic attack of HO2-, CH3OO-, PMS, and PAA might prefer to occur on the carbonyl carbons, which have more positive atomic charges. Carbon 102-109 heme oxygenase 2 Homo sapiens 37-40 35533403-7 2022 For TCBQ, the chlorine atoms cause the olefinic carbons to carry more positive atomic charges, and then, HO2- preferred to add to the olefinic carbons, which might induce the formation of the hydroxyl radical ( OH). Chloranil 4-8 heme oxygenase 2 Homo sapiens 105-108 35533403-7 2022 For TCBQ, the chlorine atoms cause the olefinic carbons to carry more positive atomic charges, and then, HO2- preferred to add to the olefinic carbons, which might induce the formation of the hydroxyl radical ( OH). Chlorine 14-22 heme oxygenase 2 Homo sapiens 105-108 35533403-7 2022 For TCBQ, the chlorine atoms cause the olefinic carbons to carry more positive atomic charges, and then, HO2- preferred to add to the olefinic carbons, which might induce the formation of the hydroxyl radical ( OH). Carbon 48-55 heme oxygenase 2 Homo sapiens 105-108 35533403-7 2022 For TCBQ, the chlorine atoms cause the olefinic carbons to carry more positive atomic charges, and then, HO2- preferred to add to the olefinic carbons, which might induce the formation of the hydroxyl radical ( OH). Carbon 143-150 heme oxygenase 2 Homo sapiens 105-108 35533403-7 2022 For TCBQ, the chlorine atoms cause the olefinic carbons to carry more positive atomic charges, and then, HO2- preferred to add to the olefinic carbons, which might induce the formation of the hydroxyl radical ( OH). Hydroxyl Radical 192-208 heme oxygenase 2 Homo sapiens 105-108 35428017-7 2022 HO-1 expression in SW480 was increased with all hemin concentrations and HO-2 expression was downregulated at the highest hemin concentration. Hemin 122-127 heme oxygenase 2 Homo sapiens 73-77 35428017-2 2022 The aim of this study was to investigate the role of heme in HO-1 and HO-2 induced colorectal carcinogenesis and the clinicopathological significance of their expressions in patients with colorectal carcinoma (CRC). Heme 53-57 heme oxygenase 2 Homo sapiens 70-74 35428017-12 2022 CONCLUSION: HO-1 and HO-2 expression is respectively induced and repressed by exogenous hemin in normal colon and colon cancer cells. Hemin 88-93 heme oxygenase 2 Homo sapiens 21-25 35428017-3 2022 METHODS: HO-1 and HO-2 expression alterations in normal colonic epithelial (FHC) and colon cancer cells (SW480) were explored following treatment with 0 microM, 25 microM, 100 microM and 250 microM concentrations of hemin, using qPCR. Hemin 216-221 heme oxygenase 2 Homo sapiens 18-22 35428017-6 2022 RESULTS: Low concentrations of hemin caused upregulation and high concentration caused downregulation of HO-1 expression, whereas HO-2 expression was significantly downregulated with all hemin concentrations in FHC. Hemin 187-192 heme oxygenase 2 Homo sapiens 130-134 35571814-8 2022 The main reactions that inhibit temperature rise are R53 (H + CH3(+M) < = > CH4(+M)), R36 (H + O2 + H2O < = > HO2 + H2O), and R46 (H + HO2 < = > O2 + H2). Oxygen 95-97 heme oxygenase 2 Homo sapiens 135-138 35571814-8 2022 The main reactions that inhibit temperature rise are R53 (H + CH3(+M) < = > CH4(+M)), R36 (H + O2 + H2O < = > HO2 + H2O), and R46 (H + HO2 < = > O2 + H2). Oxygen 145-147 heme oxygenase 2 Homo sapiens 110-113 35571814-8 2022 The main reactions that inhibit temperature rise are R53 (H + CH3(+M) < = > CH4(+M)), R36 (H + O2 + H2O < = > HO2 + H2O), and R46 (H + HO2 < = > O2 + H2). Deuterium 150-152 heme oxygenase 2 Homo sapiens 110-113 35317236-13 2022 Once the radical is quenched, it can be regenerated via the oxidations by superoxide O2 - and hydroperoxyl radical HO2 . Hydroperoxy radical 95-115 heme oxygenase 2 Homo sapiens 116-119 35496493-4 2022 The optimized structures of the reactants, intermediates and transition states involved in the reaction of the bicyclic peroxy radical with HO2 are shown. Oxygen 120-134 heme oxygenase 2 Homo sapiens 140-143 34699344-3 2022 Prospective studies are needed to identify risk predictors for home oxygen(HO2) use after curative lung cancer surgery. Oxygen 68-74 heme oxygenase 2 Homo sapiens 75-78 2492791-15 1989 SODK143 is also inactivated by HO2- by an affinity mechanism, i.e., one where reversible binding of H2O2 (HO2-) is a prerequisite for inactivation. Hydrogen Peroxide 100-104 heme oxygenase 2 Homo sapiens 31-34 35029613-6 2022 A core mechanism for the iron-catalyzed decomposition of H2O2 is proposed that is consistent with the principle of detailed balancing and includes both the one-electron oxidation of H2O2 by Fe(III) and the Fe(II) reduction of HO2 . Iron 25-29 heme oxygenase 2 Homo sapiens 226-229 35029613-6 2022 A core mechanism for the iron-catalyzed decomposition of H2O2 is proposed that is consistent with the principle of detailed balancing and includes both the one-electron oxidation of H2O2 by Fe(III) and the Fe(II) reduction of HO2 . Hydrogen Peroxide 57-61 heme oxygenase 2 Homo sapiens 226-229 2492791-20 1989 It appears that the positive charge of arginine-143 plays a role in the binding of HO2- at the active site of human Cu,ZnSOD, and that replacement of the arginine by lysine gives an enzyme with a similar affinity mechanism of inactivation, but with a greatly reduced affinity for HO2-. Lysine 166-172 heme oxygenase 2 Homo sapiens 280-283 35029613-6 2022 A core mechanism for the iron-catalyzed decomposition of H2O2 is proposed that is consistent with the principle of detailed balancing and includes both the one-electron oxidation of H2O2 by Fe(III) and the Fe(II) reduction of HO2 . ammonium ferrous sulfate 206-212 heme oxygenase 2 Homo sapiens 226-229 35075843-5 2022 MCM simulation results showed that the daily net reaction rate of O3 was 20x10-9 h-1, and HO2 +NO and RO2 (except CH3O2 )+NO contributed 49.0%-51.1% and 37.3%-40.2% of O3 generation, respectively. Ozone 66-68 heme oxygenase 2 Homo sapiens 90-93 35075843-5 2022 MCM simulation results showed that the daily net reaction rate of O3 was 20x10-9 h-1, and HO2 +NO and RO2 (except CH3O2 )+NO contributed 49.0%-51.1% and 37.3%-40.2% of O3 generation, respectively. Ozone 168-170 heme oxygenase 2 Homo sapiens 90-93 34978436-4 2022 The RO2 + RO2 pathway, which can be increasingly significant under low NOx and HO2/RO2 conditions, shows a lower SOA-forming potential compared to the RO2 + HO2 pathway. ro2 + 4-9 heme oxygenase 2 Homo sapiens 79-82 34978436-4 2022 The RO2 + RO2 pathway, which can be increasingly significant under low NOx and HO2/RO2 conditions, shows a lower SOA-forming potential compared to the RO2 + HO2 pathway. ro2 10-13 heme oxygenase 2 Homo sapiens 79-82 34978436-4 2022 The RO2 + RO2 pathway, which can be increasingly significant under low NOx and HO2/RO2 conditions, shows a lower SOA-forming potential compared to the RO2 + HO2 pathway. ro2 + 151-156 heme oxygenase 2 Homo sapiens 157-160 34978436-5 2022 While the traditional low-NOx chamber experiments are commonly used to represent the RO2 + HO2 pathway, this study finds that the impacts of the RO2 + RO2 pathway cannot be ignored under certain conditions. ro2 + 85-90 heme oxygenase 2 Homo sapiens 91-94 34978436-7 2022 On the global scale, the chemical transport model GEOS-Chem is used to identify regions characterized by lower surface HO2/RO2 ratios, suggesting that the RO2 + RO2 pathway is more likely to prove significant to overall SOA yields in those regions. ro2 + 155-160 heme oxygenase 2 Homo sapiens 119-122 34978436-7 2022 On the global scale, the chemical transport model GEOS-Chem is used to identify regions characterized by lower surface HO2/RO2 ratios, suggesting that the RO2 + RO2 pathway is more likely to prove significant to overall SOA yields in those regions. ro2 161-164 heme oxygenase 2 Homo sapiens 119-122 2492791-15 1989 SODK143 is also inactivated by HO2- by an affinity mechanism, i.e., one where reversible binding of H2O2 (HO2-) is a prerequisite for inactivation. Hydrogen Peroxide 100-104 heme oxygenase 2 Homo sapiens 106-109 2492791-19 1989 At elevated concentrations of H2O2, a second nonaffinity mechanism of inactivation of both SODR143 and SODK143 was found, in which a second equivalent of H2O2 reacts with the Cu,ZnSOD.HO2- complex to give a competing second-order inactivation. Hydrogen Peroxide 30-34 heme oxygenase 2 Homo sapiens 184-187 2492791-19 1989 At elevated concentrations of H2O2, a second nonaffinity mechanism of inactivation of both SODR143 and SODK143 was found, in which a second equivalent of H2O2 reacts with the Cu,ZnSOD.HO2- complex to give a competing second-order inactivation. Hydrogen Peroxide 154-158 heme oxygenase 2 Homo sapiens 184-187 2492791-20 1989 It appears that the positive charge of arginine-143 plays a role in the binding of HO2- at the active site of human Cu,ZnSOD, and that replacement of the arginine by lysine gives an enzyme with a similar affinity mechanism of inactivation, but with a greatly reduced affinity for HO2-. Arginine 39-47 heme oxygenase 2 Homo sapiens 83-86 2492791-20 1989 It appears that the positive charge of arginine-143 plays a role in the binding of HO2- at the active site of human Cu,ZnSOD, and that replacement of the arginine by lysine gives an enzyme with a similar affinity mechanism of inactivation, but with a greatly reduced affinity for HO2-. Arginine 39-47 heme oxygenase 2 Homo sapiens 280-283 3290025-9 1988 In vivo induction of HO-1 activity in the liver is accompanied by decreases in the total P-450 levels and, in a reconstituted system, cytochrome P-450b heme can be quantitatively converted to biliverdin by HO-1 and HO-2. Heme 152-156 heme oxygenase 2 Homo sapiens 215-219 3290025-9 1988 In vivo induction of HO-1 activity in the liver is accompanied by decreases in the total P-450 levels and, in a reconstituted system, cytochrome P-450b heme can be quantitatively converted to biliverdin by HO-1 and HO-2. Biliverdine 192-202 heme oxygenase 2 Homo sapiens 215-219 3508432-1 1987 Hydrocarbon oxidation in the atmosphere proceeds generally by the following sequence of reactions: hydrocarbon + OH----alkyl radical + H2O, alkyl radical + O2 (3 sigma)----alkylperoxy radical, alkylperoxy radical + NO----alkoxy radical + NO2, alkoxy radical + O2 (3 sigma)----aldehyde + HO2. Hydrocarbons 0-11 heme oxygenase 2 Homo sapiens 287-290 2971436-4 1988 The phosphate group and HO-2 of D-mannose 6-phosphate are important in the receptor-ligand interaction, HO-4 probably contributes to a lesser extent, and HO-1 seems to have no interaction. mannose-6-phosphate 32-53 heme oxygenase 2 Homo sapiens 24-28 2979721-2 1988 The electron-transfer reduction of molecular oxygen yields superoxide ion (O2.-), which reacts with proton sources to form HO2.. Oxygen 45-51 heme oxygenase 2 Homo sapiens 123-126 2979721-2 1988 The electron-transfer reduction of molecular oxygen yields superoxide ion (O2.-), which reacts with proton sources to form HO2.. Superoxides 59-69 heme oxygenase 2 Homo sapiens 123-126 2979721-2 1988 The electron-transfer reduction of molecular oxygen yields superoxide ion (O2.-), which reacts with proton sources to form HO2.. Oxygen 75-77 heme oxygenase 2 Homo sapiens 123-126 2979721-5 1988 + HO2.----H2O2 + O2), which have been determined from stopped-flow spectrophotometric decay data for HO2. Hydrogen Peroxide 10-14 heme oxygenase 2 Homo sapiens 2-5 2979721-5 1988 + HO2.----H2O2 + O2), which have been determined from stopped-flow spectrophotometric decay data for HO2. Hydrogen Peroxide 10-14 heme oxygenase 2 Homo sapiens 101-104 2979721-5 1988 + HO2.----H2O2 + O2), which have been determined from stopped-flow spectrophotometric decay data for HO2. Oxygen 3-5 heme oxygenase 2 Homo sapiens 101-104 2825650-2 1987 In neutral solutions, desferrioxamine (Desferal) can react with the superoxide free radical, O2.- (possibly through its protonated form HO2. Deferoxamine 22-37 heme oxygenase 2 Homo sapiens 136-139 2825650-2 1987 In neutral solutions, desferrioxamine (Desferal) can react with the superoxide free radical, O2.- (possibly through its protonated form HO2. Deferoxamine 39-47 heme oxygenase 2 Homo sapiens 136-139 2825650-2 1987 In neutral solutions, desferrioxamine (Desferal) can react with the superoxide free radical, O2.- (possibly through its protonated form HO2. superoxide free radical 68-91 heme oxygenase 2 Homo sapiens 136-139 2825650-2 1987 In neutral solutions, desferrioxamine (Desferal) can react with the superoxide free radical, O2.- (possibly through its protonated form HO2. Oxygen 93-95 heme oxygenase 2 Homo sapiens 136-139 2435667-7 1987 Experiments performed in the presence of various radical scavengers suggest that the inactivation of the channel is due to a combined action of OH and of HO2 radicals at the tryptophan residues. Tryptophan 174-184 heme oxygenase 2 Homo sapiens 154-157 3021842-3 1986 These results are compared to studies of the reactivity of Trolox with HO2/O2- and are discussed in light of the known antioxidant properties of vitamin E. 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid 59-65 heme oxygenase 2 Homo sapiens 71-74 3460064-3 1986 The pH dependence and rate-limiting second-order rate constants (kly) for oxygen transfer from H2O2 and HO2- to the iron(III) porphyrin were determined by trapping of the resultant higher-valent iron-oxo porphyrin species with 2,2"-azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS). Oxygen 74-80 heme oxygenase 2 Homo sapiens 104-107 3460064-3 1986 The pH dependence and rate-limiting second-order rate constants (kly) for oxygen transfer from H2O2 and HO2- to the iron(III) porphyrin were determined by trapping of the resultant higher-valent iron-oxo porphyrin species with 2,2"-azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS). iron(iii) porphyrin 116-135 heme oxygenase 2 Homo sapiens 104-107 3460064-3 1986 The pH dependence and rate-limiting second-order rate constants (kly) for oxygen transfer from H2O2 and HO2- to the iron(III) porphyrin were determined by trapping of the resultant higher-valent iron-oxo porphyrin species with 2,2"-azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS). iron-oxo porphyrin 195-213 heme oxygenase 2 Homo sapiens 104-107 3460064-3 1986 The pH dependence and rate-limiting second-order rate constants (kly) for oxygen transfer from H2O2 and HO2- to the iron(III) porphyrin were determined by trapping of the resultant higher-valent iron-oxo porphyrin species with 2,2"-azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS). 2,2"-azinodi(3-ethylbenzthiazoline)-6-sulfonate 227-274 heme oxygenase 2 Homo sapiens 104-107 3460064-3 1986 The pH dependence and rate-limiting second-order rate constants (kly) for oxygen transfer from H2O2 and HO2- to the iron(III) porphyrin were determined by trapping of the resultant higher-valent iron-oxo porphyrin species with 2,2"-azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS). ABTS diammonium salt 276-280 heme oxygenase 2 Homo sapiens 104-107 3005043-3 1986 The presence of tris(picolinato)manganese(II) [MnII(PA)2(PAH)(H2O)], a model complex for mitochondrial superoxide dismutase, (i) efficiently catalyzes the disproportionation of O2.-, (ii) precludes the formation HO2., and thereby (iii) prevents hydrogen abstraction from allylic and thiol groups. tris(picolinato)manganese 16-41 heme oxygenase 2 Homo sapiens 212-215 3005043-3 1986 The presence of tris(picolinato)manganese(II) [MnII(PA)2(PAH)(H2O)], a model complex for mitochondrial superoxide dismutase, (i) efficiently catalyzes the disproportionation of O2.-, (ii) precludes the formation HO2., and thereby (iii) prevents hydrogen abstraction from allylic and thiol groups. p-Aminohippuric Acid 57-60 heme oxygenase 2 Homo sapiens 212-215 3005043-3 1986 The presence of tris(picolinato)manganese(II) [MnII(PA)2(PAH)(H2O)], a model complex for mitochondrial superoxide dismutase, (i) efficiently catalyzes the disproportionation of O2.-, (ii) precludes the formation HO2., and thereby (iii) prevents hydrogen abstraction from allylic and thiol groups. Water 62-65 heme oxygenase 2 Homo sapiens 212-215 3886800-12 1985 The results of experiments with scavengers of oxygen reduction intermediates and of nitroblue tetrazolium reduction tests indicated that H2O2, O2- and 1O2 were involved in the killing of AMA by LF-treated MPM. Nitroblue Tetrazolium 84-105 heme oxygenase 2 Homo sapiens 137-154 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. Water 53-56 heme oxygenase 2 Homo sapiens 204-207 6097242-2 1984 Solutions prepared in the presence of atmospheric oxygen at pH = 12 exhibited a typical semiquinone signal preceded by a short-lived signal attributed to perhydroxyl radical, HO2. Oxygen 50-56 heme oxygenase 2 Homo sapiens 175-178 6833274-0 1983 A study of the reactivity of HO2/O2- with unsaturated fatty acids. Fatty Acids, Unsaturated 42-65 heme oxygenase 2 Homo sapiens 29-32 6833274-1 1983 The reaction of perhydroxyl radical (HO2) with linoleic, linolenic, and arachidonic acids has been studied in aqueous ethanolic solutions by the stopped flow technique. perhydroxyl radical 16-35 heme oxygenase 2 Homo sapiens 37-40 6833274-1 1983 The reaction of perhydroxyl radical (HO2) with linoleic, linolenic, and arachidonic acids has been studied in aqueous ethanolic solutions by the stopped flow technique. Linoleic Acid 47-55 heme oxygenase 2 Homo sapiens 37-40 6833274-1 1983 The reaction of perhydroxyl radical (HO2) with linoleic, linolenic, and arachidonic acids has been studied in aqueous ethanolic solutions by the stopped flow technique. linolenic 57-66 heme oxygenase 2 Homo sapiens 37-40 6833274-1 1983 The reaction of perhydroxyl radical (HO2) with linoleic, linolenic, and arachidonic acids has been studied in aqueous ethanolic solutions by the stopped flow technique. Arachidonic Acids 72-89 heme oxygenase 2 Homo sapiens 37-40 6833274-3 1983 While kinetic results suggest that the HO2 radical reacts with the double allylic H atom of the polyunsaturated fatty acids, thermodynamic approximations indicate that the reaction is exothermic by approximately 10 kcal/mol. Fatty Acids, Unsaturated 96-123 heme oxygenase 2 Homo sapiens 39-42 6833274-4 1983 The relevance of this reaction to membrane damage observed in biological systems that have been exposed to HO2/O2- radicals is discussed. o2- radicals 111-123 heme oxygenase 2 Homo sapiens 107-110 600809-2 1977 We fing the most probable causes of poor 99mTc-labeling in these cases to be: a) the presence of a large concentration of 99TcO4-in eluants; b) insufficient stannous ions available for the complete reduction of Tc due to spontaneous oxidation of Sn in the vial and also due to oxidation of stannous ions by the presence of larger than expected concentrations of H2O2 and HO2 radicals in the eluant. Technetium 44-46 heme oxygenase 2 Homo sapiens 371-374 241106-1 1975 Rotating ring-disc electrode studies have indicated that relatively large quantities of hydrogen peroxide ion, HO2-, are produced when oxygen is reduced at a platinum or gold polarographic electrode surface. Hydrogen Peroxide 88-105 heme oxygenase 2 Homo sapiens 111-114 241106-1 1975 Rotating ring-disc electrode studies have indicated that relatively large quantities of hydrogen peroxide ion, HO2-, are produced when oxygen is reduced at a platinum or gold polarographic electrode surface. Oxygen 135-141 heme oxygenase 2 Homo sapiens 111-114 237890-0 1975 Kinetic study by pulse radiolysis of the lactate dehydrogenase-catalyzed chain oxidation of nicotinamide adenine dinucleotide by HO2 and O2-RADICALS. NAD 92-125 heme oxygenase 2 Homo sapiens 129-132 237890-1 1975 The lactate dehydrogenase-catalyzed chain oxidation of NADH (LDH-NADH) by the superoxide radicals, HO2 and O2, has been studied with pulse radiolysis in the pH range between 4.5 and 9.0. NAD 55-59 heme oxygenase 2 Homo sapiens 99-102 237890-1 1975 The lactate dehydrogenase-catalyzed chain oxidation of NADH (LDH-NADH) by the superoxide radicals, HO2 and O2, has been studied with pulse radiolysis in the pH range between 4.5 and 9.0. NAD 65-69 heme oxygenase 2 Homo sapiens 99-102 237890-1 1975 The lactate dehydrogenase-catalyzed chain oxidation of NADH (LDH-NADH) by the superoxide radicals, HO2 and O2, has been studied with pulse radiolysis in the pH range between 4.5 and 9.0. Superoxides 78-88 heme oxygenase 2 Homo sapiens 99-102 237890-2 1975 The rate constants for the oxidation of the LDH-NADH by HO2 and O2 determined at 23 degrees are 1.2 times 10-6 M(-1) s(-1) and 3.6 times 10-4 M(-1) s(-1), respectively. NAD 48-52 heme oxygenase 2 Homo sapiens 56-59 33927054-2 2021 Our analysis of a 2012 airborne study of deep convection and chemistry demonstrates that lightning also directly generates the oxidants OH and the hydroperoxyl radical (HO2). Hydroperoxy radical 147-167 heme oxygenase 2 Homo sapiens 169-172 6097141-0 1984 Reevaluation of the reactivity of hydroxylamine with O2-/HO2. Hydroxylamine 34-47 heme oxygenase 2 Homo sapiens 57-60 6097141-1 1984 The reactivity of hydroxylamine with HO2/O2- radicals was studied by pulse radiolysis and stopped-flow photolysis over a pH range of 1.1-10.5. Hydroxylamine 18-31 heme oxygenase 2 Homo sapiens 37-40 6097141-1 1984 The reactivity of hydroxylamine with HO2/O2- radicals was studied by pulse radiolysis and stopped-flow photolysis over a pH range of 1.1-10.5. o2- radicals 41-53 heme oxygenase 2 Homo sapiens 37-40 6314839-4 1983 As these solutions can be rendered free of molecular oxygen, studies of the reactivity of HO2/O-2 with oxygen-sensitive compounds under virtually anaerobic conditions are possible. Oxygen 53-59 heme oxygenase 2 Homo sapiens 90-97 6314839-4 1983 As these solutions can be rendered free of molecular oxygen, studies of the reactivity of HO2/O-2 with oxygen-sensitive compounds under virtually anaerobic conditions are possible. Oxygen 103-109 heme oxygenase 2 Homo sapiens 90-97 6799200-5 1982 The resonance of HO-2 of the uronate residue of chondrosinate also shows anomalies that may arise from intra-residue hydrogen-bonding. Uronic Acids 29-36 heme oxygenase 2 Homo sapiens 17-21 6799200-5 1982 The resonance of HO-2 of the uronate residue of chondrosinate also shows anomalies that may arise from intra-residue hydrogen-bonding. chondrosinate 48-61 heme oxygenase 2 Homo sapiens 17-21 6799200-5 1982 The resonance of HO-2 of the uronate residue of chondrosinate also shows anomalies that may arise from intra-residue hydrogen-bonding. Hydrogen 117-125 heme oxygenase 2 Homo sapiens 17-21 42252-8 1979 b) Molecular oxygen was reduced to HO2- and H2O2, respectively. Oxygen 13-19 heme oxygenase 2 Homo sapiens 35-38 9199-4 1976 Thus, the aglycon group in the alpha anomers protects position 3, the axial HO-4 in galactopyranosides protects position 2, and the axial HO-2 in mannopyranosides protects position 4 from oxidation. Mannose 146-162 heme oxygenase 2 Homo sapiens 138-142 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. Formyl chloride 61-76 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. ch2clo 182-188 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. Oxygen 191-193 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. Hydrochloric Acid 79-82 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. Water 223-226 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. cmhp 266-270 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. Water 223-226 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. ch2clo 301-307 heme oxygenase 2 Homo sapiens 204-207 33949520-4 2021 At a later time of the reaction, absorption bands of H2O and formyl chloride (CHClO) at 1782.9 cm-1 were observed; these species were likely produced from the secondary reactions of CH2ClO + O2 CHClO + HO2 and OH + HCl H2O + Cl according to temporal profiles of CMHP, H2O, and CHClO; formation of CH2ClO + OH via decomposition of internally excited CMHP was predicted by theory and both HCl and O2 are major species in the system. cmhp 353-357 heme oxygenase 2 Homo sapiens 204-207 32638314-4 2021 This is due to the generation of photo-active reactive oxygen species (HO and HO2 -/O2 -) under photolysis in STP effluent, as verified by experiments in the presence of 2-propanol and chloroform. Oxygen 55-61 heme oxygenase 2 Homo sapiens 79-82 32638314-4 2021 This is due to the generation of photo-active reactive oxygen species (HO and HO2 -/O2 -) under photolysis in STP effluent, as verified by experiments in the presence of 2-propanol and chloroform. 2-Propanol 171-181 heme oxygenase 2 Homo sapiens 79-82 32638314-4 2021 This is due to the generation of photo-active reactive oxygen species (HO and HO2 -/O2 -) under photolysis in STP effluent, as verified by experiments in the presence of 2-propanol and chloroform. Chloroform 186-196 heme oxygenase 2 Homo sapiens 79-82 33387762-6 2021 Carbonyls played a vital role in both the primary formation and recycling of the ROx; more than 80% of the primary source of HO2 and RO2 came from photolysis of formaldehyde and other oxygenated VOCs. Formaldehyde 161-173 heme oxygenase 2 Homo sapiens 125-128 33864218-3 2021 Approximately 82% of As(III) oxidation was attributed to HO which depended strongly on HO2 /O2 -. as(iii) 21-28 heme oxygenase 2 Homo sapiens 88-91 33492594-4 2021 Predictions for the photolytic and UVC/H2O2 processes confirmed the good agreement with experimental data, enabling the estimation of fundamental kinetic parameters, such as the direct photolysis quantum yield (F254 nm, Zn-Bc = 0.0143 mol Einstein-1) and the second-order rate constants for the reactions of Zn-Bc with HO , HO2 , and O2 - radicals (2.64 x 109, 1.63 x 103, and 1.49 x 104 L mol-1 s-1, respectively). Hydrogen Peroxide 39-43 heme oxygenase 2 Homo sapiens 324-327 33492594-4 2021 Predictions for the photolytic and UVC/H2O2 processes confirmed the good agreement with experimental data, enabling the estimation of fundamental kinetic parameters, such as the direct photolysis quantum yield (F254 nm, Zn-Bc = 0.0143 mol Einstein-1) and the second-order rate constants for the reactions of Zn-Bc with HO , HO2 , and O2 - radicals (2.64 x 109, 1.63 x 103, and 1.49 x 104 L mol-1 s-1, respectively). Bacitracin 220-225 heme oxygenase 2 Homo sapiens 324-327 33870420-2 2021 Heme oxygenase is the rate-limiting enzyme in heme metabolism; heme oxygenase-2 (HO-2) is a constitutively expressed heme oxygenase. Heme 46-50 heme oxygenase 2 Homo sapiens 81-85 33870420-2 2021 Heme oxygenase is the rate-limiting enzyme in heme metabolism; heme oxygenase-2 (HO-2) is a constitutively expressed heme oxygenase. Heme 63-67 heme oxygenase 2 Homo sapiens 81-85 33387762-7 2021 Zero-out sensitivity studies showed that the seven measured carbonyls accounted for 37% of the peak net O3 production rate, mainly by affecting the concentrations of HO2 and RO2. Ozone 104-106 heme oxygenase 2 Homo sapiens 166-169 33338865-9 2021 For example, the amount of OH determined by the Weissler and Fricke methods may have some uncertainty due to the formation of HO2 in the presence of oxygen. Oxygen 149-155 heme oxygenase 2 Homo sapiens 126-129 33637263-9 2021 Physical contribution, including horizontal transport and vertical transport, may pose uncertainties on the indication of O3 formation regime by HO2/OH ratio. Ozone 122-124 heme oxygenase 2 Homo sapiens 145-151 33637263-10 2021 In comparison with other commonly used photochemical indicators, HO2/OH ratio had the best performance in differentiating O3 formation regimes. Ozone 122-124 heme oxygenase 2 Homo sapiens 65-71 33637263-7 2021 Over eastern PRD, O3 formation was mainly in a NOx-limited regime when HO2/OH ratio was higher than 11, while in a VOC-limited regime when the ratio was lower than 9.5. Ozone 18-20 heme oxygenase 2 Homo sapiens 71-77 33713713-5 2021 Furthermore, HO2 /O2 - was helpful in removing anthracene and fluoranthene. Oxygen 18-22 heme oxygenase 2 Homo sapiens 13-16 33704337-9 2021 The HO2- % was as low as 0.59% and current density was 4.9 mA cm-2 at 0.2 V (Vs. RHE) on the plasma-treated NiCo2O4. nico2o4 108-115 heme oxygenase 2 Homo sapiens 4-7 33729087-8 2021 The amount of total oxidation reactions caused by oxidative ROS, such as OH and hydroperoxyl radial (HO2 ), was decreased with increasing LET. Reactive Oxygen Species 60-63 heme oxygenase 2 Homo sapiens 102-105 33729087-8 2021 The amount of total oxidation reactions caused by oxidative ROS, such as OH and hydroperoxyl radial (HO2 ), was decreased with increasing LET. hydroperoxyl radial 81-100 heme oxygenase 2 Homo sapiens 102-105 33713713-5 2021 Furthermore, HO2 /O2 - was helpful in removing anthracene and fluoranthene. anthracene 47-57 heme oxygenase 2 Homo sapiens 13-16 33713713-5 2021 Furthermore, HO2 /O2 - was helpful in removing anthracene and fluoranthene. fluoranthene 62-74 heme oxygenase 2 Homo sapiens 13-16 33742855-7 2021 Through the analysis of chemical reaction mechanisms, it is concluded that VOCs and CO affect the photochemical reaction by reacting with OH, HO2 and other free radicals, which causes the significant interaction between VOCs and CO in the generation of ozone. Ozone 253-258 heme oxygenase 2 Homo sapiens 142-145 33560846-1 2021 In low-temperature flash photolysis of NH3/O2/N2 mixtures, the NH2 consumption rate and the product distribution is controlled by the reactions NH2 + HO2 products (R1), NH2 + H (+M) NH3 (+M) (R2), and NH2 + NH2 (+M) N2H4 (+M) (R3). Ammonia 39-42 heme oxygenase 2 Homo sapiens 150-153 33560846-1 2021 In low-temperature flash photolysis of NH3/O2/N2 mixtures, the NH2 consumption rate and the product distribution is controlled by the reactions NH2 + HO2 products (R1), NH2 + H (+M) NH3 (+M) (R2), and NH2 + NH2 (+M) N2H4 (+M) (R3). Oxygen 43-45 heme oxygenase 2 Homo sapiens 150-153 33560846-1 2021 In low-temperature flash photolysis of NH3/O2/N2 mixtures, the NH2 consumption rate and the product distribution is controlled by the reactions NH2 + HO2 products (R1), NH2 + H (+M) NH3 (+M) (R2), and NH2 + NH2 (+M) N2H4 (+M) (R3). Nitrogen 46-48 heme oxygenase 2 Homo sapiens 150-153 33560846-1 2021 In low-temperature flash photolysis of NH3/O2/N2 mixtures, the NH2 consumption rate and the product distribution is controlled by the reactions NH2 + HO2 products (R1), NH2 + H (+M) NH3 (+M) (R2), and NH2 + NH2 (+M) N2H4 (+M) (R3). Amido radical 63-66 heme oxygenase 2 Homo sapiens 150-153 33560846-1 2021 In low-temperature flash photolysis of NH3/O2/N2 mixtures, the NH2 consumption rate and the product distribution is controlled by the reactions NH2 + HO2 products (R1), NH2 + H (+M) NH3 (+M) (R2), and NH2 + NH2 (+M) N2H4 (+M) (R3). hydrazine 222-226 heme oxygenase 2 Homo sapiens 150-153 33560846-8 2021 Measured HNO profiles indicate that this component is formed directly by NH2 + HO2 HNO + H2O (R1b), but theoretical work indicates that R1b is only a minor channel. nitroxyl 9-12 heme oxygenase 2 Homo sapiens 79-82 33560846-8 2021 Measured HNO profiles indicate that this component is formed directly by NH2 + HO2 HNO + H2O (R1b), but theoretical work indicates that R1b is only a minor channel. Amido radical 73-76 heme oxygenase 2 Homo sapiens 79-82 33560846-8 2021 Measured HNO profiles indicate that this component is formed directly by NH2 + HO2 HNO + H2O (R1b), but theoretical work indicates that R1b is only a minor channel. nitroxyl 85-88 heme oxygenase 2 Homo sapiens 79-82 33560846-8 2021 Measured HNO profiles indicate that this component is formed directly by NH2 + HO2 HNO + H2O (R1b), but theoretical work indicates that R1b is only a minor channel. Water 91-94 heme oxygenase 2 Homo sapiens 79-82 33268062-8 2021 An electron transfer of the Mn species facilitated the decomposition of PS to generate HO2 /O2 - radicals, which were utilized as a precursor for 1O2 generation via direct oxidation or the recombination of HO2 /O2 -. ps 72-74 heme oxygenase 2 Homo sapiens 87-90 33268062-8 2021 An electron transfer of the Mn species facilitated the decomposition of PS to generate HO2 /O2 - radicals, which were utilized as a precursor for 1O2 generation via direct oxidation or the recombination of HO2 /O2 -. ps 72-74 heme oxygenase 2 Homo sapiens 207-210 33268062-8 2021 An electron transfer of the Mn species facilitated the decomposition of PS to generate HO2 /O2 - radicals, which were utilized as a precursor for 1O2 generation via direct oxidation or the recombination of HO2 /O2 -. Oxygen 92-97 heme oxygenase 2 Homo sapiens 87-90 33268062-8 2021 An electron transfer of the Mn species facilitated the decomposition of PS to generate HO2 /O2 - radicals, which were utilized as a precursor for 1O2 generation via direct oxidation or the recombination of HO2 /O2 -. Oxygen 92-97 heme oxygenase 2 Homo sapiens 207-210 33268062-8 2021 An electron transfer of the Mn species facilitated the decomposition of PS to generate HO2 /O2 - radicals, which were utilized as a precursor for 1O2 generation via direct oxidation or the recombination of HO2 /O2 -. CHEBI:63768 147-150 heme oxygenase 2 Homo sapiens 87-90 33268062-8 2021 An electron transfer of the Mn species facilitated the decomposition of PS to generate HO2 /O2 - radicals, which were utilized as a precursor for 1O2 generation via direct oxidation or the recombination of HO2 /O2 -. CHEBI:63768 147-150 heme oxygenase 2 Homo sapiens 207-210 33268062-8 2021 An electron transfer of the Mn species facilitated the decomposition of PS to generate HO2 /O2 - radicals, which were utilized as a precursor for 1O2 generation via direct oxidation or the recombination of HO2 /O2 -. Oxygen 212-217 heme oxygenase 2 Homo sapiens 87-90 33557324-2 2021 Quasi-reversible O2/O2 - redox was found to be modified by the compounds, suggesting that an acid-base reaction in which a hydroperoxyl radical (HO2 ) is formed from O2 - occurs. Oxygen 17-19 heme oxygenase 2 Homo sapiens 145-148 33557324-2 2021 Quasi-reversible O2/O2 - redox was found to be modified by the compounds, suggesting that an acid-base reaction in which a hydroperoxyl radical (HO2 ) is formed from O2 - occurs. Oxygen 20-22 heme oxygenase 2 Homo sapiens 145-148 33557324-2 2021 Quasi-reversible O2/O2 - redox was found to be modified by the compounds, suggesting that an acid-base reaction in which a hydroperoxyl radical (HO2 ) is formed from O2 - occurs. Hydroperoxy radical 123-143 heme oxygenase 2 Homo sapiens 145-148 33557324-2 2021 Quasi-reversible O2/O2 - redox was found to be modified by the compounds, suggesting that an acid-base reaction in which a hydroperoxyl radical (HO2 ) is formed from O2 - occurs. Oxygen 20-22 heme oxygenase 2 Homo sapiens 145-148 33360083-6 2021 O2- /HO2 and OH were responsible for the cathodic TC degradation. Oxygen 0-2 heme oxygenase 2 Homo sapiens 5-8 33360083-6 2021 O2- /HO2 and OH were responsible for the cathodic TC degradation. Tetracycline 52-54 heme oxygenase 2 Homo sapiens 5-8 33417765-5 2021 We demonstrated that the synergistic effect of multiple reactive species originated from tandem cascade reactions comprising reduction of O2 by H to form O2 -/HO2 and downstream reaction of O2 - with NO to yield ONOO-. Oxygen 138-140 heme oxygenase 2 Homo sapiens 160-163 33417765-5 2021 We demonstrated that the synergistic effect of multiple reactive species originated from tandem cascade reactions comprising reduction of O2 by H to form O2 -/HO2 and downstream reaction of O2 - with NO to yield ONOO-. Oxygen 155-157 heme oxygenase 2 Homo sapiens 160-163 33417765-5 2021 We demonstrated that the synergistic effect of multiple reactive species originated from tandem cascade reactions comprising reduction of O2 by H to form O2 -/HO2 and downstream reaction of O2 - with NO to yield ONOO-. Oxygen 155-157 heme oxygenase 2 Homo sapiens 160-163 33417765-5 2021 We demonstrated that the synergistic effect of multiple reactive species originated from tandem cascade reactions comprising reduction of O2 by H to form O2 -/HO2 and downstream reaction of O2 - with NO to yield ONOO-. onoo 215-219 heme oxygenase 2 Homo sapiens 160-163 33051205-6 2020 We find that, under heme-deficient conditions, HO2 is destabilized and targeted for degradation, suggesting heme plays a direct role in HO2 regulation. Heme 108-112 heme oxygenase 2 Homo sapiens 47-50 33550277-3 2021 Using Univariable Cox regression analysis and Lasso regression analysis method in the training dataset, it was found that the four DNA methylation markers (CCNT1, ITGB3, SDS, and HMOX2) were significantly correlated with the overall survival of patients with PDAC. Sodium Dodecyl Sulfate 170-173 heme oxygenase 2 Homo sapiens 179-184 33183711-3 2021 In the atmosphere and troposphere, hydroperoxyl radicals (HO2) are closely demanded in the chemical oxidation of the troposphere. hydroperoxyl radicals 35-56 heme oxygenase 2 Homo sapiens 58-61 33183711-7 2021 The primary goal of this review is to deepen our understanding of the functions of the most critical free radical ( OH, HO2) and also understand the currently used methods to quantify them in the atmosphere and troposphere. Free Radicals 101-113 heme oxygenase 2 Homo sapiens 120-123 33051205-0 2020 Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site. Heme 54-58 heme oxygenase 2 Homo sapiens 0-16 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Heme 45-49 heme oxygenase 2 Homo sapiens 0-16 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Heme 45-49 heme oxygenase 2 Homo sapiens 18-21 33051205-6 2020 We find that, under heme-deficient conditions, HO2 is destabilized and targeted for degradation, suggesting heme plays a direct role in HO2 regulation. Heme 108-112 heme oxygenase 2 Homo sapiens 136-139 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Biliverdine 65-75 heme oxygenase 2 Homo sapiens 0-16 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Biliverdine 65-75 heme oxygenase 2 Homo sapiens 18-21 33051205-7 2020 HO2 has three heme binding sites: one at its catalytic site, and the others at its two heme regulatory motifs (HRMs). Heme 14-18 heme oxygenase 2 Homo sapiens 0-3 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Carbon Monoxide 77-79 heme oxygenase 2 Homo sapiens 0-16 33051205-7 2020 HO2 has three heme binding sites: one at its catalytic site, and the others at its two heme regulatory motifs (HRMs). Heme 87-91 heme oxygenase 2 Homo sapiens 0-3 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Carbon Monoxide 77-79 heme oxygenase 2 Homo sapiens 18-21 33051205-10 2020 Consistently, a HO2 catalytic site variant that is unable to bind heme exhibits a constant low protein level and an enhanced protein degradation rate compared to the wild-type HO2. Heme 66-70 heme oxygenase 2 Homo sapiens 16-19 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Iron 85-89 heme oxygenase 2 Homo sapiens 0-16 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Iron 85-89 heme oxygenase 2 Homo sapiens 18-21 33051205-12 2020 These results reveal a novel aspect of HO2 regulation and deepen our understanding of HO2"s role in maintaining heme homeostasis, paving the way for future investigation into HO2"s pathophysiological role in heme deficiency response. Heme 112-116 heme oxygenase 2 Homo sapiens 86-89 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Heme 124-128 heme oxygenase 2 Homo sapiens 0-16 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Heme 124-128 heme oxygenase 2 Homo sapiens 18-21 33051205-2 2020 Tight regulation of the cellular levels and catalytic activities of HO1 and HO2 is important for maintaining heme homeostasis. Heme 109-113 heme oxygenase 2 Homo sapiens 76-79 33051205-5 2020 Here, we elucidate the mechanism of post-translational regulation of cellular HO2 levels by heme. Heme 92-96 heme oxygenase 2 Homo sapiens 78-81 33051205-6 2020 We find that, under heme-deficient conditions, HO2 is destabilized and targeted for degradation, suggesting heme plays a direct role in HO2 regulation. Heme 20-24 heme oxygenase 2 Homo sapiens 47-50 33051205-6 2020 We find that, under heme-deficient conditions, HO2 is destabilized and targeted for degradation, suggesting heme plays a direct role in HO2 regulation. Heme 20-24 heme oxygenase 2 Homo sapiens 136-139 33051205-12 2020 These results reveal a novel aspect of HO2 regulation and deepen our understanding of HO2"s role in maintaining heme homeostasis, paving the way for future investigation into HO2"s pathophysiological role in heme deficiency response. Heme 112-116 heme oxygenase 2 Homo sapiens 86-89 33231595-6 2020 Three different product complexes, ketene HO2, ketene H2O HO2 and ketene (H2O)2 HO2, are formed from the reaction. Water 54-57 heme oxygenase 2 Homo sapiens 58-61 33231595-6 2020 Three different product complexes, ketene HO2, ketene H2O HO2 and ketene (H2O)2 HO2, are formed from the reaction. Water 54-57 heme oxygenase 2 Homo sapiens 58-61 32569955-2 2020 In this work, UVA radiation that is part of solar light is taken as the irradiation source and radicals (HO, SO4- and HO2/O2-) are generated through activation of hydrogen peroxide (H2O2), sodium persulfate (Na2S2O8) and Bismuth catalyst (BiOCl), respectively. Hydrogen Peroxide 163-180 heme oxygenase 2 Homo sapiens 118-126 33251447-7 2020 Further analysis concluded that the substituted CO2 has the greatest influence on the LBV sensitivity coefficient of the HO2 + CH3 = OH + CH3O reaction. Carbon Dioxide 48-51 heme oxygenase 2 Homo sapiens 121-124 33251447-7 2020 Further analysis concluded that the substituted CO2 has the greatest influence on the LBV sensitivity coefficient of the HO2 + CH3 = OH + CH3O reaction. 7-methoxy-6-(2'-methoxy-3'-hydroxy-3'-methyl butyl) 138-142 heme oxygenase 2 Homo sapiens 121-124 33084314-6 2020 Similarly, the reaction of BCP-peroxy with HO2 largely recycles HOx, producing the corresponding bicyclic alkoxy radical (BCP-oxy). bicyclic alkoxy radical 97-120 heme oxygenase 2 Homo sapiens 43-46 33084314-6 2020 Similarly, the reaction of BCP-peroxy with HO2 largely recycles HOx, producing the corresponding bicyclic alkoxy radical (BCP-oxy). bcp-oxy 122-129 heme oxygenase 2 Homo sapiens 43-46 32569955-2 2020 In this work, UVA radiation that is part of solar light is taken as the irradiation source and radicals (HO, SO4- and HO2/O2-) are generated through activation of hydrogen peroxide (H2O2), sodium persulfate (Na2S2O8) and Bismuth catalyst (BiOCl), respectively. Hydrogen Peroxide 182-186 heme oxygenase 2 Homo sapiens 118-126 32569955-2 2020 In this work, UVA radiation that is part of solar light is taken as the irradiation source and radicals (HO, SO4- and HO2/O2-) are generated through activation of hydrogen peroxide (H2O2), sodium persulfate (Na2S2O8) and Bismuth catalyst (BiOCl), respectively. sodium persulfate 189-206 heme oxygenase 2 Homo sapiens 118-126 32569955-2 2020 In this work, UVA radiation that is part of solar light is taken as the irradiation source and radicals (HO, SO4- and HO2/O2-) are generated through activation of hydrogen peroxide (H2O2), sodium persulfate (Na2S2O8) and Bismuth catalyst (BiOCl), respectively. sodium persulfate 208-215 heme oxygenase 2 Homo sapiens 118-126 32569955-2 2020 In this work, UVA radiation that is part of solar light is taken as the irradiation source and radicals (HO, SO4- and HO2/O2-) are generated through activation of hydrogen peroxide (H2O2), sodium persulfate (Na2S2O8) and Bismuth catalyst (BiOCl), respectively. Bismuth 221-228 heme oxygenase 2 Homo sapiens 118-126 32569955-2 2020 In this work, UVA radiation that is part of solar light is taken as the irradiation source and radicals (HO, SO4- and HO2/O2-) are generated through activation of hydrogen peroxide (H2O2), sodium persulfate (Na2S2O8) and Bismuth catalyst (BiOCl), respectively. bismuth oxychloride 239-244 heme oxygenase 2 Homo sapiens 118-126 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. Heme 29-33 heme oxygenase 2 Homo sapiens 58-74 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. Heme 29-33 heme oxygenase 2 Homo sapiens 76-81 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. ammonium ferrous sulfate 130-134 heme oxygenase 2 Homo sapiens 58-74 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. Carbon Monoxide 113-128 heme oxygenase 2 Homo sapiens 58-74 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. ammonium ferrous sulfate 130-134 heme oxygenase 2 Homo sapiens 76-81 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. Carbon Monoxide 113-128 heme oxygenase 2 Homo sapiens 76-81 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. Biliverdine 139-149 heme oxygenase 2 Homo sapiens 58-74 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. Biliverdine 139-149 heme oxygenase 2 Homo sapiens 76-81 32852951-5 2020 An increase in the rate of the HO2 self-reaction was also observed as a function of acetone (CH3C(O)CH3) concentration which is interpreted as a chaperone effect resulting from hydrogen-bond complexation between HO2 and CH3C(O)CH3. Acetone 84-91 heme oxygenase 2 Homo sapiens 212-215 32585482-11 2020 RO2 + HO2 pathway derived 2-methyltetrols (2-MTs) predominated the EFs of isoprene-derived products (SOAi) in the fresh samples. ro2 + 0-5 heme oxygenase 2 Homo sapiens 6-9 32585482-11 2020 RO2 + HO2 pathway derived 2-methyltetrols (2-MTs) predominated the EFs of isoprene-derived products (SOAi) in the fresh samples. 2-methyltetrols 26-41 heme oxygenase 2 Homo sapiens 6-9 32585482-11 2020 RO2 + HO2 pathway derived 2-methyltetrols (2-MTs) predominated the EFs of isoprene-derived products (SOAi) in the fresh samples. isoprene 74-82 heme oxygenase 2 Homo sapiens 6-9 32860873-3 2020 Endogenously, CO is synthesized upon degradation of heme by heme oxygenases (HOs) of which two enzymatically active isoenzymes are known in mammals; the stress-inducible HO-1 and the constitutively expressed HO-2. Carbon Monoxide 14-16 heme oxygenase 2 Homo sapiens 208-212 32860873-3 2020 Endogenously, CO is synthesized upon degradation of heme by heme oxygenases (HOs) of which two enzymatically active isoenzymes are known in mammals; the stress-inducible HO-1 and the constitutively expressed HO-2. Heme 52-56 heme oxygenase 2 Homo sapiens 208-212 32852951-1 2020 Pulsed laser photolysis coupled with infrared (IR) wavelength modulation spectroscopy and ultraviolet (UV) absorption spectroscopy was used to study the kinetics and branching fractions for the acetonyl peroxy (CH3C(O)CH2O2) self-reaction and its reaction with hydro peroxy (HO2) at a temperature of 298 K and pressure of 100 Torr. acetonyl peroxy 194-209 heme oxygenase 2 Homo sapiens 275-278 32852951-1 2020 Pulsed laser photolysis coupled with infrared (IR) wavelength modulation spectroscopy and ultraviolet (UV) absorption spectroscopy was used to study the kinetics and branching fractions for the acetonyl peroxy (CH3C(O)CH2O2) self-reaction and its reaction with hydro peroxy (HO2) at a temperature of 298 K and pressure of 100 Torr. ch3c(o)ch2o2 211-223 heme oxygenase 2 Homo sapiens 275-278 32852951-3 2020 The overall rate constant for the reaction between CH3C(O)CH2O2 and HO2 was found to be (5.5 +- 0.5) x 10^-12 cm^3 molecule-1 s^-1 and the branching fraction for OH yield from this reaction was directly measured as 0.30 +- 0.04. formic acid 58-63 heme oxygenase 2 Homo sapiens 68-71 32852951-5 2020 An increase in the rate of the HO2 self-reaction was also observed as a function of acetone (CH3C(O)CH3) concentration which is interpreted as a chaperone effect resulting from hydrogen-bond complexation between HO2 and CH3C(O)CH3. Acetone 84-91 heme oxygenase 2 Homo sapiens 31-34 32852951-5 2020 An increase in the rate of the HO2 self-reaction was also observed as a function of acetone (CH3C(O)CH3) concentration which is interpreted as a chaperone effect resulting from hydrogen-bond complexation between HO2 and CH3C(O)CH3. Hydrogen 177-185 heme oxygenase 2 Homo sapiens 31-34 32852951-5 2020 An increase in the rate of the HO2 self-reaction was also observed as a function of acetone (CH3C(O)CH3) concentration which is interpreted as a chaperone effect resulting from hydrogen-bond complexation between HO2 and CH3C(O)CH3. Hydrogen 177-185 heme oxygenase 2 Homo sapiens 212-215 32862648-9 2020 The calculations showed that unimolecular elimination of hydroperoxyl radical (HO2) from the RO2 adduct through formation of propanethial is a major reaction under atmospherically relevant conditions. Hydroperoxy radical 57-77 heme oxygenase 2 Homo sapiens 79-82 32862648-9 2020 The calculations showed that unimolecular elimination of hydroperoxyl radical (HO2) from the RO2 adduct through formation of propanethial is a major reaction under atmospherically relevant conditions. ro2 93-96 heme oxygenase 2 Homo sapiens 79-82 32862648-9 2020 The calculations showed that unimolecular elimination of hydroperoxyl radical (HO2) from the RO2 adduct through formation of propanethial is a major reaction under atmospherically relevant conditions. propanethial 125-137 heme oxygenase 2 Homo sapiens 79-82 32862648-10 2020 The overall results suggest that the atmospheric removal of DPTS is mainly due to reactions with OH and 3O2, resulting in formation of propanesulfinic acid, propanethial, HO2, and sulfur dioxide (SO2) as the major products. diphenylthiosulfinate 60-64 heme oxygenase 2 Homo sapiens 172-175 32862648-10 2020 The overall results suggest that the atmospheric removal of DPTS is mainly due to reactions with OH and 3O2, resulting in formation of propanesulfinic acid, propanethial, HO2, and sulfur dioxide (SO2) as the major products. CHEMBL1771216 105-108 heme oxygenase 2 Homo sapiens 172-175 32519538-8 2020 The hydroxycyclohexadienylperoxy radical produced in this reaction can eliminate hydroperoxyl radical (HO2 ) to produce a phenolic compound or it can rearrange to form a bicyclic peroxy intermediate that subsequently undergoes ring cleavage. hydroxycyclohexadienylperoxy radical 4-40 heme oxygenase 2 Homo sapiens 103-106 33003730-1 2020 We report a synchrotron radiation vacuum ultraviolet photoionization study of the hydroperoxyl radical (HO2), a key reaction intermediate in combustion and atmospheric chemistry as well as astrochemistry, using double imaging photoelectron photoion coincidence spectroscopy. Hydroperoxy radical 82-102 heme oxygenase 2 Homo sapiens 104-107 33003730-2 2020 The HO2 radical is formed in a microwave discharge flow tube reactor through a set of reactions initiated by F atoms in a CH4/O2/He gas mixture. Methane 122-125 heme oxygenase 2 Homo sapiens 4-7 33003730-2 2020 The HO2 radical is formed in a microwave discharge flow tube reactor through a set of reactions initiated by F atoms in a CH4/O2/He gas mixture. Helium 129-131 heme oxygenase 2 Homo sapiens 4-7 32557062-0 2020 Atmospheric chemistry of CF2ClO2: a theoretical study on mechanisms and kinetics of the CF2ClO2 + HO2 reaction. cf2clo2 25-32 heme oxygenase 2 Homo sapiens 98-101 32557062-0 2020 Atmospheric chemistry of CF2ClO2: a theoretical study on mechanisms and kinetics of the CF2ClO2 + HO2 reaction. cf2clo2 88-95 heme oxygenase 2 Homo sapiens 98-101 32557062-1 2020 The singlet and triplet potential energy surfaces of the HO2 with CF2ClO2 reaction have been probed at the BMC-CCSD/cc-pVTZ level according to the B3LYP/6-311++G(d,p) level obtained geometrical structure. cf2clo2 66-73 heme oxygenase 2 Homo sapiens 57-60 32806915-8 2020 However, HO2 produced via the oxygen reduction reaction in the EO process plays a major role in As(III) oxidation, which explains the lower reaction rate in the absence of S(IV). Oxygen 31-37 heme oxygenase 2 Homo sapiens 9-12 32806915-8 2020 However, HO2 produced via the oxygen reduction reaction in the EO process plays a major role in As(III) oxidation, which explains the lower reaction rate in the absence of S(IV). as(iii) 97-104 heme oxygenase 2 Homo sapiens 9-12 32627769-10 2020 We propose a sequence of ion-molecule and radical reactions to explain the formation of O2-, HO2- and other ions observed in the negatively charged cluster ion series. Oxygen 88-90 heme oxygenase 2 Homo sapiens 93-96 32844841-7 2020 At all conditions studied, the recombination of gamma-isobutanol radical with O2 forms HO2 + isobutanal. gamma-isobutanol 48-64 heme oxygenase 2 Homo sapiens 87-90 32844841-7 2020 At all conditions studied, the recombination of gamma-isobutanol radical with O2 forms HO2 + isobutanal. Oxygen 78-80 heme oxygenase 2 Homo sapiens 87-90 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. beta-isobutanol 21-36 heme oxygenase 2 Homo sapiens 165-168 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. beta-isobutanol 21-36 heme oxygenase 2 Homo sapiens 371-374 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. Oxygen 50-52 heme oxygenase 2 Homo sapiens 165-168 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. Oxygen 50-52 heme oxygenase 2 Homo sapiens 371-374 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. Alkenes 174-180 heme oxygenase 2 Homo sapiens 165-168 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. beta-isobutanol 216-231 heme oxygenase 2 Homo sapiens 371-374 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. Acetone 309-316 heme oxygenase 2 Homo sapiens 371-374 32844841-8 2020 The recombination of beta-isobutanol radical with O2 forms a stabilized hydroperoxy alkyl radical below 400 K, water + an alkoxy radical at higher temperatures, and HO2 + an alkene above 1200 K. The recombination of beta-isobutanol radical with O2 results in a mixture of products between 700-1100 K, forming acetone + formaldehyde + OH at lower temperatures and forming HO2 + alkenes at higher temperatures. Formaldehyde 319-331 heme oxygenase 2 Homo sapiens 371-374 32963690-7 2020 At these sites with the higher acidity, the chance of protonation of the superoxide radical (O2 ), generated by the respiratory chain, is much higher with the formation of the highly reactive hydrophobic perhydroxyl radical (HO2 ). Superoxides 73-91 heme oxygenase 2 Homo sapiens 226-229 32963690-7 2020 At these sites with the higher acidity, the chance of protonation of the superoxide radical (O2 ), generated by the respiratory chain, is much higher with the formation of the highly reactive hydrophobic perhydroxyl radical (HO2 ). Oxygen 93-95 heme oxygenase 2 Homo sapiens 226-229 32963690-7 2020 At these sites with the higher acidity, the chance of protonation of the superoxide radical (O2 ), generated by the respiratory chain, is much higher with the formation of the highly reactive hydrophobic perhydroxyl radical (HO2 ). perhydroxyl radical 205-224 heme oxygenase 2 Homo sapiens 226-229 32963690-8 2020 HO2 specifically reacts with the double bonds of polyunsaturated fatty acids (PUFA) initiating the isoprostane pathway of lipid peroxidation. Fatty Acids, Unsaturated 51-78 heme oxygenase 2 Homo sapiens 0-3 32963690-8 2020 HO2 specifically reacts with the double bonds of polyunsaturated fatty acids (PUFA) initiating the isoprostane pathway of lipid peroxidation. Fatty Acids, Unsaturated 80-84 heme oxygenase 2 Homo sapiens 0-3 32963690-8 2020 HO2 specifically reacts with the double bonds of polyunsaturated fatty acids (PUFA) initiating the isoprostane pathway of lipid peroxidation. Isoprostanes 101-112 heme oxygenase 2 Homo sapiens 0-3 32963690-9 2020 Because HO2 is formed close to CL aggregates and PEA, it causes peroxidation of the linoleic acid in CL and also damages PEA. Linoleic Acid 86-99 heme oxygenase 2 Homo sapiens 8-11 32963690-11 2020 We provide evidence that in elderly individuals with metabolic syndrome (MetS), fatty acids become the major substrates for production of ATP and this may increase several-fold generation of O2 and thus HO2 . Fatty Acids 80-91 heme oxygenase 2 Homo sapiens 205-208 32963690-11 2020 We provide evidence that in elderly individuals with metabolic syndrome (MetS), fatty acids become the major substrates for production of ATP and this may increase several-fold generation of O2 and thus HO2 . Adenosine Triphosphate 138-141 heme oxygenase 2 Homo sapiens 205-208 32557062-3 2020 On the triplet PES, SN2 displacement and indirect H- abstraction reaction mechanisms have been investigated and the H- abstraction channel makes more contribution to the CF2ClO2 with HO2 reaction. cf2clo2 170-177 heme oxygenase 2 Homo sapiens 183-186 32557062-6 2020 The predicted data for CF2ClO2 + HO2 agrees closely with available experimental value. cf2clo2 23-30 heme oxygenase 2 Homo sapiens 33-36 32982786-5 2020 HO-1 and HO-2 catalyze the rate-limiting step of cellular heme degradation and, similar to SirT1, HO-1 exerts beneficial effects in the vasculature through the activation of anti-oxidant, anti-inflammatory, anti-apoptotic, and anti-proliferative signaling pathways. Heme 58-62 heme oxygenase 2 Homo sapiens 9-13 32417560-6 2020 The species-specific second order rate constants for the reactions of H2O2 with HOI, HO2- with HOI, and HO2- with OI- were determined as kH2O2+HOI = 29 +- 5.2 M-1s-1, kHO2-+HOI = (3.1 +- 0.3) x 108 M-1s-1, and kHO2-+OI- = (6.4 +- 1.4) x 107 M-1s-1, respectively. Hydrogen Peroxide 70-74 heme oxygenase 2 Homo sapiens 85-88 32417560-6 2020 The species-specific second order rate constants for the reactions of H2O2 with HOI, HO2- with HOI, and HO2- with OI- were determined as kH2O2+HOI = 29 +- 5.2 M-1s-1, kHO2-+HOI = (3.1 +- 0.3) x 108 M-1s-1, and kHO2-+OI- = (6.4 +- 1.4) x 107 M-1s-1, respectively. Hydrogen Peroxide 70-74 heme oxygenase 2 Homo sapiens 104-107 32417560-6 2020 The species-specific second order rate constants for the reactions of H2O2 with HOI, HO2- with HOI, and HO2- with OI- were determined as kH2O2+HOI = 29 +- 5.2 M-1s-1, kHO2-+HOI = (3.1 +- 0.3) x 108 M-1s-1, and kHO2-+OI- = (6.4 +- 1.4) x 107 M-1s-1, respectively. kh2o2 137-142 heme oxygenase 2 Homo sapiens 85-88 32417560-6 2020 The species-specific second order rate constants for the reactions of H2O2 with HOI, HO2- with HOI, and HO2- with OI- were determined as kH2O2+HOI = 29 +- 5.2 M-1s-1, kHO2-+HOI = (3.1 +- 0.3) x 108 M-1s-1, and kHO2-+OI- = (6.4 +- 1.4) x 107 M-1s-1, respectively. kh2o2 137-142 heme oxygenase 2 Homo sapiens 104-107 32519538-8 2020 The hydroxycyclohexadienylperoxy radical produced in this reaction can eliminate hydroperoxyl radical (HO2 ) to produce a phenolic compound or it can rearrange to form a bicyclic peroxy intermediate that subsequently undergoes ring cleavage. Hydroperoxy radical 81-101 heme oxygenase 2 Homo sapiens 103-106 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Ozone 30-32 heme oxygenase 2 Homo sapiens 35-38 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Ozone 30-32 heme oxygenase 2 Homo sapiens 175-178 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Ozone 30-32 heme oxygenase 2 Homo sapiens 175-178 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 46-50 heme oxygenase 2 Homo sapiens 35-38 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 46-50 heme oxygenase 2 Homo sapiens 175-178 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 46-50 heme oxygenase 2 Homo sapiens 175-178 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 36-38 heme oxygenase 2 Homo sapiens 175-178 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 36-38 heme oxygenase 2 Homo sapiens 175-178 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 46-48 heme oxygenase 2 Homo sapiens 35-38 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 46-48 heme oxygenase 2 Homo sapiens 175-178 32685808-6 2020 On the contrary, the reaction O3 + HO2 = OH + O2 + O2 has a significant effect on the explosion limit in the high-pressure and low-temperature region, as the concentration of HO2 increases through the rapid third-body reaction H + O2 + M = HO2 + M. Oxygen 46-48 heme oxygenase 2 Homo sapiens 175-178 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. ch2clooocl 58-68 heme oxygenase 2 Homo sapiens 201-204 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. chcl2ooocl 75-85 heme oxygenase 2 Homo sapiens 179-182 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. ch2clooocl 58-68 heme oxygenase 2 Homo sapiens 179-182 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. chcl2ooocl 75-85 heme oxygenase 2 Homo sapiens 201-204 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. chclo 171-176 heme oxygenase 2 Homo sapiens 179-182 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. chclo 171-176 heme oxygenase 2 Homo sapiens 201-204 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. ccl2o 193-198 heme oxygenase 2 Homo sapiens 179-182 32242320-4 2020 RRKM calculations presented that the initial adducts IM1 (CH2ClOOOCl)/IM1 (CHCl2OOOCl) are the primary products at T < 400 K and T < 600 K, respectively, and products P1 (CHClO + HO2 + Cl)/P1 (CCl2O + HO2 + Cl) are dominant the reactions at T >= 400 K and T >= 600 K, respectively. ccl2o 193-198 heme oxygenase 2 Homo sapiens 201-204 32152224-0 2020 The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation. Heme 4-8 heme oxygenase 2 Homo sapiens 30-46 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Disulfides 108-117 heme oxygenase 2 Homo sapiens 36-52 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Disulfides 108-117 heme oxygenase 2 Homo sapiens 54-57 32294377-6 2020 We find that HONO photolysis is the dominant contributor to hydrogen oxide radicals (HOx = OH + HO2) in early stage (< 3 hours) wildfire plume evolution. Nitrous Acid 13-17 heme oxygenase 2 Homo sapiens 96-99 32294377-6 2020 We find that HONO photolysis is the dominant contributor to hydrogen oxide radicals (HOx = OH + HO2) in early stage (< 3 hours) wildfire plume evolution. hydrogen oxide radicals 60-83 heme oxygenase 2 Homo sapiens 96-99 32298086-3 2020 Reactive oxygen species (ROS) including OH, HO2 and 1O2 are proposed to be the main oxidants of the PI/HA system, which is supported by various tests employing the scavengers, chemical probes, and spin-trapping electron paramagnetic resonance (EPR) technique. Reactive Oxygen Species 0-23 heme oxygenase 2 Homo sapiens 45-57 32298086-3 2020 Reactive oxygen species (ROS) including OH, HO2 and 1O2 are proposed to be the main oxidants of the PI/HA system, which is supported by various tests employing the scavengers, chemical probes, and spin-trapping electron paramagnetic resonance (EPR) technique. Reactive Oxygen Species 25-28 heme oxygenase 2 Homo sapiens 45-57 32298086-3 2020 Reactive oxygen species (ROS) including OH, HO2 and 1O2 are proposed to be the main oxidants of the PI/HA system, which is supported by various tests employing the scavengers, chemical probes, and spin-trapping electron paramagnetic resonance (EPR) technique. Hydroxylamine 105-107 heme oxygenase 2 Homo sapiens 45-57 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Cysteine 144-153 heme oxygenase 2 Homo sapiens 36-52 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Cysteine 144-153 heme oxygenase 2 Homo sapiens 54-57 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Cysteine 83-91 heme oxygenase 2 Homo sapiens 36-52 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Cysteine 83-91 heme oxygenase 2 Homo sapiens 54-57 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. fe3+-heme 176-185 heme oxygenase 2 Homo sapiens 36-52 31983006-6 2020 The reaction of peroxy radical intermediate with HO2 and NOx (x = 1, 2) radicals is studied in detail. adenylyl 5'-peroxydiphosphate 16-22 heme oxygenase 2 Homo sapiens 49-60 32152224-2 2020 The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. fe3+-heme 176-185 heme oxygenase 2 Homo sapiens 54-57 32152224-4 2020 Here, we describe the reversible, protein-mediated transfer of heme between the HRMs and the HO2 core. Heme 63-67 heme oxygenase 2 Homo sapiens 93-96 32152224-5 2020 Using hydrogen-deuterium exchange (HDX)-MS to monitor the dynamics of HO2 with and without Fe3+-heme bound to the HRMs and to the core, we detected conformational changes in the catalytic core only in one state of the catalytic cycle-when Fe3+-heme is bound to the HRMs and the core is in the apo state. Hydrogen 6-14 heme oxygenase 2 Homo sapiens 70-73 32152224-5 2020 Using hydrogen-deuterium exchange (HDX)-MS to monitor the dynamics of HO2 with and without Fe3+-heme bound to the HRMs and to the core, we detected conformational changes in the catalytic core only in one state of the catalytic cycle-when Fe3+-heme is bound to the HRMs and the core is in the apo state. Deuterium 15-24 heme oxygenase 2 Homo sapiens 70-73 32152224-5 2020 Using hydrogen-deuterium exchange (HDX)-MS to monitor the dynamics of HO2 with and without Fe3+-heme bound to the HRMs and to the core, we detected conformational changes in the catalytic core only in one state of the catalytic cycle-when Fe3+-heme is bound to the HRMs and the core is in the apo state. fe3+-heme 239-248 heme oxygenase 2 Homo sapiens 70-73 31865128-3 2020 The inside mechanism of the LFUA process includes: 1) displacement of HMIs from HMI-EDTA complexes by Fe(III); 2) direct photolysis of Fe(III)-EDTA through a ligand-to-metal charge transition reaction (LMCT) and indirect photolysis of EDTA by HO2 /O2 -. isothiocyanobenzyl ethylenediamine tetracetic acid 84-88 heme oxygenase 2 Homo sapiens 243-246 31865128-3 2020 The inside mechanism of the LFUA process includes: 1) displacement of HMIs from HMI-EDTA complexes by Fe(III); 2) direct photolysis of Fe(III)-EDTA through a ligand-to-metal charge transition reaction (LMCT) and indirect photolysis of EDTA by HO2 /O2 -. Iron 102-109 heme oxygenase 2 Homo sapiens 243-246 31865128-3 2020 The inside mechanism of the LFUA process includes: 1) displacement of HMIs from HMI-EDTA complexes by Fe(III); 2) direct photolysis of Fe(III)-EDTA through a ligand-to-metal charge transition reaction (LMCT) and indirect photolysis of EDTA by HO2 /O2 -. EDDA 135-147 heme oxygenase 2 Homo sapiens 243-246 31865128-3 2020 The inside mechanism of the LFUA process includes: 1) displacement of HMIs from HMI-EDTA complexes by Fe(III); 2) direct photolysis of Fe(III)-EDTA through a ligand-to-metal charge transition reaction (LMCT) and indirect photolysis of EDTA by HO2 /O2 -. isothiocyanobenzyl ethylenediamine tetracetic acid 143-147 heme oxygenase 2 Homo sapiens 243-246 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. Iron 0-6 heme oxygenase 2 Homo sapiens 94-97 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. EDDA 42-54 heme oxygenase 2 Homo sapiens 94-97 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. Iron 42-49 heme oxygenase 2 Homo sapiens 94-97 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. Iron 76-83 heme oxygenase 2 Homo sapiens 94-97 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. isothiocyanobenzyl ethylenediamine tetracetic acid 50-54 heme oxygenase 2 Homo sapiens 94-97 31922747-2 2020 Hydrogen atom transfer (HAT) by 3O2 and HO2 from arenols (ArOH), aryloxyls (ArO ), their tautomers (ArH), and auxiliary compounds has been investigated by means of CBS-QB3 computations. Hydrogen 0-8 heme oxygenase 2 Homo sapiens 40-43 32035862-2 2020 In living organisms, it is produced endogenously during the degradation of heme by oxygenase, which occurs in three isoforms: HO-1, HO-2 and HO-3. Heme 75-79 heme oxygenase 2 Homo sapiens 132-136 31977206-9 2020 The change of the O2/fuel ratio from 0.5 to 2.0 lead to an increase of CO2 formation mainly from O2 + O=COH CO2 + HO2 and O2 + CO CO2 + O reactions. Superoxides 18-20 heme oxygenase 2 Homo sapiens 116-119 31977206-9 2020 The change of the O2/fuel ratio from 0.5 to 2.0 lead to an increase of CO2 formation mainly from O2 + O=COH CO2 + HO2 and O2 + CO CO2 + O reactions. Carbon Dioxide 71-74 heme oxygenase 2 Homo sapiens 116-119 31977206-9 2020 The change of the O2/fuel ratio from 0.5 to 2.0 lead to an increase of CO2 formation mainly from O2 + O=COH CO2 + HO2 and O2 + CO CO2 + O reactions. Superoxides 72-74 heme oxygenase 2 Homo sapiens 116-119 31977206-9 2020 The change of the O2/fuel ratio from 0.5 to 2.0 lead to an increase of CO2 formation mainly from O2 + O=COH CO2 + HO2 and O2 + CO CO2 + O reactions. Carbon Dioxide 110-113 heme oxygenase 2 Homo sapiens 116-119 31977206-9 2020 The change of the O2/fuel ratio from 0.5 to 2.0 lead to an increase of CO2 formation mainly from O2 + O=COH CO2 + HO2 and O2 + CO CO2 + O reactions. Superoxides 72-74 heme oxygenase 2 Homo sapiens 116-119 31977206-9 2020 The change of the O2/fuel ratio from 0.5 to 2.0 lead to an increase of CO2 formation mainly from O2 + O=COH CO2 + HO2 and O2 + CO CO2 + O reactions. Carbon Dioxide 71-73 heme oxygenase 2 Homo sapiens 116-119 31977206-9 2020 The change of the O2/fuel ratio from 0.5 to 2.0 lead to an increase of CO2 formation mainly from O2 + O=COH CO2 + HO2 and O2 + CO CO2 + O reactions. Carbon Dioxide 110-113 heme oxygenase 2 Homo sapiens 116-119 32105282-0 2020 Reaction pathways and kinetics study on a syngas combustion system: CO + HO2 in an H2O environment. Water 83-86 heme oxygenase 2 Homo sapiens 73-76 32105282-1 2020 The reaction between CO and HO2 plays a significant role in syngas combustion. Carbon Monoxide 21-23 heme oxygenase 2 Homo sapiens 28-31 32105282-3 2020 Firstly, the potential energy surface (PES) of CO + HO2 (water-free) is revisited. Water 57-62 heme oxygenase 2 Homo sapiens 52-55 32105282-5 2020 In the presence of water, the title reaction has three different pre-reactive complexes (i.e., RC2: COHO2 + H2O, RC3: COH2O + HO2, and RC4: HO2H2O + CO), depending on the initial hydrogen bond formation. Water 19-24 heme oxygenase 2 Homo sapiens 102-105 31812525-8 2020 The generation of OH and HO2/ O2- radicals in the bulk solution was crucial to phenol degradation, and the decomposition of H2O2 complied with the pseudo-first-order kinetics. Phenol 81-87 heme oxygenase 2 Homo sapiens 27-30 31812525-8 2020 The generation of OH and HO2/ O2- radicals in the bulk solution was crucial to phenol degradation, and the decomposition of H2O2 complied with the pseudo-first-order kinetics. Hydrogen Peroxide 126-130 heme oxygenase 2 Homo sapiens 27-30 31922747-2 2020 Hydrogen atom transfer (HAT) by 3O2 and HO2 from arenols (ArOH), aryloxyls (ArO ), their tautomers (ArH), and auxiliary compounds has been investigated by means of CBS-QB3 computations. arenols 50-57 heme oxygenase 2 Homo sapiens 40-43 31922747-2 2020 Hydrogen atom transfer (HAT) by 3O2 and HO2 from arenols (ArOH), aryloxyls (ArO ), their tautomers (ArH), and auxiliary compounds has been investigated by means of CBS-QB3 computations. aroh 59-63 heme oxygenase 2 Homo sapiens 40-43 31922747-2 2020 Hydrogen atom transfer (HAT) by 3O2 and HO2 from arenols (ArOH), aryloxyls (ArO ), their tautomers (ArH), and auxiliary compounds has been investigated by means of CBS-QB3 computations. aro 59-62 heme oxygenase 2 Homo sapiens 40-43 31922747-7 2020 A kinetic analysis shows that the HAT by chain-carrying HO2 occurs with a high rate constant of >=6 x 108 M-1 s-1 (toluene). Toluene 116-123 heme oxygenase 2 Homo sapiens 56-59 31922747-9 2020 Oxanthrone (AnOH) is a more stable tautomer of AnH2Q with a ratio of 13 (298 K) in non-hydrogen-bonding (HB) solvents, but the reactivity toward 3O2/HO2 is much lower. OXANTHRONE 0-10 heme oxygenase 2 Homo sapiens 149-152 31922747-9 2020 Oxanthrone (AnOH) is a more stable tautomer of AnH2Q with a ratio of 13 (298 K) in non-hydrogen-bonding (HB) solvents, but the reactivity toward 3O2/HO2 is much lower. anoh 12-16 heme oxygenase 2 Homo sapiens 149-152 31922747-10 2020 Combination of the computed free energies and Abrahams" HB donating (alpha2H) and accepting (beta2H) parameters has afforded an alpha2H(HO2 ) of 0.86 and an alpha2H(H2O2) of 0.50. alpha2h 69-76 heme oxygenase 2 Homo sapiens 136-139 31922747-10 2020 Combination of the computed free energies and Abrahams" HB donating (alpha2H) and accepting (beta2H) parameters has afforded an alpha2H(HO2 ) of 0.86 and an alpha2H(H2O2) of 0.50. beta2h 93-99 heme oxygenase 2 Homo sapiens 136-139 31922747-10 2020 Combination of the computed free energies and Abrahams" HB donating (alpha2H) and accepting (beta2H) parameters has afforded an alpha2H(HO2 ) of 0.86 and an alpha2H(H2O2) of 0.50. alpha2h 128-135 heme oxygenase 2 Homo sapiens 136-139 31922747-10 2020 Combination of the computed free energies and Abrahams" HB donating (alpha2H) and accepting (beta2H) parameters has afforded an alpha2H(HO2 ) of 0.86 and an alpha2H(H2O2) of 0.50. alpha2h 128-135 heme oxygenase 2 Homo sapiens 136-139 31922747-10 2020 Combination of the computed free energies and Abrahams" HB donating (alpha2H) and accepting (beta2H) parameters has afforded an alpha2H(HO2 ) of 0.86 and an alpha2H(H2O2) of 0.50. Hydrogen Peroxide 165-169 heme oxygenase 2 Homo sapiens 136-139 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 16-21 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 16-21 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Oxygen 58-64 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Oxygen 58-64 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 138-143 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 138-143 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Superoxides 166-168 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Superoxides 166-168 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 16-20 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 16-20 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Water 220-225 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Water 220-225 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Superoxides 202-204 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 138-143 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 138-143 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 138-142 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . NADP 138-142 heme oxygenase 2 Homo sapiens 304-307 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Water 363-368 heme oxygenase 2 Homo sapiens 201-204 31713255-7 2020 The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP+ and HO2 - , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2 + , which further reacts with NADPH to yield NADP+ and H2 O2 . Water 363-368 heme oxygenase 2 Homo sapiens 304-307 31528950-5 2019 In addition, the rate constant was calculated for the favorable initial OH-addition reactions over the temperature range of 278 to 1000 K. The subsequent reactions for the favorable BNA-OH adduct intermediate with O2, HO2 and NO radicals are studied. 2-bromo-4,6-dinitroaniline 182-185 heme oxygenase 2 Homo sapiens 218-221 32064385-10 2020 The computational efficiency and beneficial scaling of the method allow for application to larger systems, as shown for hydrogen abstraction from 2-butanone by HO2 . Hydrogen 120-128 heme oxygenase 2 Homo sapiens 160-163 32064385-10 2020 The computational efficiency and beneficial scaling of the method allow for application to larger systems, as shown for hydrogen abstraction from 2-butanone by HO2 . methylethyl ketone 146-156 heme oxygenase 2 Homo sapiens 160-163 31912066-7 2020 The detected product ions, corresponding to loss of OH + CO2, OH + HCHO, HO2 , and HO2 + CO2 from the peroxyl radical, can all be reconciled by the proposed reaction mechanism. perhydroxyl radical 105-112 heme oxygenase 2 Homo sapiens 75-78 31912066-7 2020 The detected product ions, corresponding to loss of OH + CO2, OH + HCHO, HO2 , and HO2 + CO2 from the peroxyl radical, can all be reconciled by the proposed reaction mechanism. perhydroxyl radical 105-112 heme oxygenase 2 Homo sapiens 85-88 31670037-6 2020 Moreover, the intermediates P7H, P9H, and P10H could easily transform to several stable products in the presence of O2, HO2 , and OH. p7h 28-31 heme oxygenase 2 Homo sapiens 120-123 31670037-6 2020 Moreover, the intermediates P7H, P9H, and P10H could easily transform to several stable products in the presence of O2, HO2 , and OH. (2~{S})-2-azanyl-5-[[(2~{R})-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-3-[(1~{R})-3-oxidanylidene-1-phenyl-propyl]sulfanyl-propan-2-yl]amino]-5-oxidanylidene-pentanoic acid 33-36 heme oxygenase 2 Homo sapiens 120-123 31670037-6 2020 Moreover, the intermediates P7H, P9H, and P10H could easily transform to several stable products in the presence of O2, HO2 , and OH. p10h 42-46 heme oxygenase 2 Homo sapiens 120-123 31670037-7 2020 The peroxy radical, which is generated from the incorporation of H-abstraction product radicals (P7H, P9H, and P10H) with O2, prefers to produce HO2 into the surrounding through direct concerted elimination rather than the indirect mechanism. Oxygen 4-18 heme oxygenase 2 Homo sapiens 145-148 31670037-7 2020 The peroxy radical, which is generated from the incorporation of H-abstraction product radicals (P7H, P9H, and P10H) with O2, prefers to produce HO2 into the surrounding through direct concerted elimination rather than the indirect mechanism. h-abstraction product radicals 65-95 heme oxygenase 2 Homo sapiens 145-148 31670037-7 2020 The peroxy radical, which is generated from the incorporation of H-abstraction product radicals (P7H, P9H, and P10H) with O2, prefers to produce HO2 into the surrounding through direct concerted elimination rather than the indirect mechanism. p7h 97-100 heme oxygenase 2 Homo sapiens 145-148 31670037-7 2020 The peroxy radical, which is generated from the incorporation of H-abstraction product radicals (P7H, P9H, and P10H) with O2, prefers to produce HO2 into the surrounding through direct concerted elimination rather than the indirect mechanism. (2~{S})-2-azanyl-5-[[(2~{R})-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-3-[(1~{R})-3-oxidanylidene-1-phenyl-propyl]sulfanyl-propan-2-yl]amino]-5-oxidanylidene-pentanoic acid 102-105 heme oxygenase 2 Homo sapiens 145-148 31670037-7 2020 The peroxy radical, which is generated from the incorporation of H-abstraction product radicals (P7H, P9H, and P10H) with O2, prefers to produce HO2 into the surrounding through direct concerted elimination rather than the indirect mechanism. p10h 111-115 heme oxygenase 2 Homo sapiens 145-148 31670037-7 2020 The peroxy radical, which is generated from the incorporation of H-abstraction product radicals (P7H, P9H, and P10H) with O2, prefers to produce HO2 into the surrounding through direct concerted elimination rather than the indirect mechanism. Oxygen 122-124 heme oxygenase 2 Homo sapiens 145-148 31693359-0 2019 Understanding the spatial heterogeneity of indoor OH and HO2 due to photolysis of HONO using Computational Fluid Dynamics (CFD) simulation. Nitrous Acid 82-86 heme oxygenase 2 Homo sapiens 57-60 31693359-4 2019 The results showed that OH and HO2 were essentially confined in the volume of HONO-photolyzing light, but oxidation products were relatively well distributed throughout the room. Nitrous Acid 78-82 heme oxygenase 2 Homo sapiens 31-34 31550661-6 2019 To the best of our knowledge, among HO-2 inhibitors, clemizole derivatives are the most selective HO-2 inhibitors reported so far (IC50 HO-1 >100 muM, IC50 HO-2 = 3.4 muM), while the HO-2 nonselective inhibitors described herein possess IC50 HO-2 values <= 10 muM. clemizole 53-62 heme oxygenase 2 Homo sapiens 98-102 31727545-12 2019 DISCUSSION: Increase in non-haem iron prior to induction of HO-1 expression suggests the involvement of HO-2 in haem-induced cytotoxicity. Iron 33-37 heme oxygenase 2 Homo sapiens 104-108 31646308-0 2019 Atmospheric chemistry of the self-reaction of HO2 radicals: stepwise mechanism versus one-step process in the presence of (H2O)n (n = 1-3) clusters. Water 123-126 heme oxygenase 2 Homo sapiens 46-49 31646308-2 2019 In the present work, the HO2 + HO2 reactions with (H2O)n (n = 1-3) have been investigated using quantum chemical methods and canonical variational transition state theory with small curvature tunneling. Water 51-54 heme oxygenase 2 Homo sapiens 25-28 31646308-2 2019 In the present work, the HO2 + HO2 reactions with (H2O)n (n = 1-3) have been investigated using quantum chemical methods and canonical variational transition state theory with small curvature tunneling. Water 51-54 heme oxygenase 2 Homo sapiens 31-34 31601767-2 2019 Here, we report a direct electrosynthesis strategy that delivers separate hydrogen (H2) and oxygen (O2) streams to an anode and cathode separated by a porous solid electrolyte, wherein the electrochemically generated H+ and HO2 - recombine to form pure aqueous H2O2 solutions. Hydrogen 74-82 heme oxygenase 2 Homo sapiens 224-227 31601767-2 2019 Here, we report a direct electrosynthesis strategy that delivers separate hydrogen (H2) and oxygen (O2) streams to an anode and cathode separated by a porous solid electrolyte, wherein the electrochemically generated H+ and HO2 - recombine to form pure aqueous H2O2 solutions. Hydrogen 84-86 heme oxygenase 2 Homo sapiens 224-227 31601767-2 2019 Here, we report a direct electrosynthesis strategy that delivers separate hydrogen (H2) and oxygen (O2) streams to an anode and cathode separated by a porous solid electrolyte, wherein the electrochemically generated H+ and HO2 - recombine to form pure aqueous H2O2 solutions. Oxygen 92-98 heme oxygenase 2 Homo sapiens 224-227 31601767-2 2019 Here, we report a direct electrosynthesis strategy that delivers separate hydrogen (H2) and oxygen (O2) streams to an anode and cathode separated by a porous solid electrolyte, wherein the electrochemically generated H+ and HO2 - recombine to form pure aqueous H2O2 solutions. Oxygen 100-102 heme oxygenase 2 Homo sapiens 224-227 31601767-2 2019 Here, we report a direct electrosynthesis strategy that delivers separate hydrogen (H2) and oxygen (O2) streams to an anode and cathode separated by a porous solid electrolyte, wherein the electrochemically generated H+ and HO2 - recombine to form pure aqueous H2O2 solutions. Hydrogen Peroxide 261-265 heme oxygenase 2 Homo sapiens 224-227 31936545-7 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 83-89 heme oxygenase 2 Homo sapiens 39-53 31936545-7 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 83-89 heme oxygenase 2 Homo sapiens 184-198 31936545-7 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 210-216 heme oxygenase 2 Homo sapiens 39-53 31936545-7 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 210-216 heme oxygenase 2 Homo sapiens 184-198 31936545-16 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 83-89 heme oxygenase 2 Homo sapiens 39-53 31936545-16 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 83-89 heme oxygenase 2 Homo sapiens 184-198 31936545-16 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 210-216 heme oxygenase 2 Homo sapiens 39-53 31936545-16 2020 The remarkable correlation between the HO 2 and O 2 - production yield and the oxygen enhancement ratio observed in biological systems suggests a direct or indirect involvement of HO 2 and O 2 - in the oxygen sensitization effect. Oxygen 210-216 heme oxygenase 2 Homo sapiens 184-198 31550661-6 2019 To the best of our knowledge, among HO-2 inhibitors, clemizole derivatives are the most selective HO-2 inhibitors reported so far (IC50 HO-1 >100 muM, IC50 HO-2 = 3.4 muM), while the HO-2 nonselective inhibitors described herein possess IC50 HO-2 values <= 10 muM. clemizole 53-62 heme oxygenase 2 Homo sapiens 36-40 31550661-6 2019 To the best of our knowledge, among HO-2 inhibitors, clemizole derivatives are the most selective HO-2 inhibitors reported so far (IC50 HO-1 >100 muM, IC50 HO-2 = 3.4 muM), while the HO-2 nonselective inhibitors described herein possess IC50 HO-2 values <= 10 muM. clemizole 53-62 heme oxygenase 2 Homo sapiens 98-102 31550661-6 2019 To the best of our knowledge, among HO-2 inhibitors, clemizole derivatives are the most selective HO-2 inhibitors reported so far (IC50 HO-1 >100 muM, IC50 HO-2 = 3.4 muM), while the HO-2 nonselective inhibitors described herein possess IC50 HO-2 values <= 10 muM. clemizole 53-62 heme oxygenase 2 Homo sapiens 98-102 31550661-6 2019 To the best of our knowledge, among HO-2 inhibitors, clemizole derivatives are the most selective HO-2 inhibitors reported so far (IC50 HO-1 >100 muM, IC50 HO-2 = 3.4 muM), while the HO-2 nonselective inhibitors described herein possess IC50 HO-2 values <= 10 muM. clemizole 53-62 heme oxygenase 2 Homo sapiens 98-102 31550661-7 2019 Furthermore, the development of HO-2 activators, such as menadione analogues, helped to understand the critical moieties required for HO-2 activation. Vitamin K 3 57-66 heme oxygenase 2 Homo sapiens 32-36 31550661-7 2019 Furthermore, the development of HO-2 activators, such as menadione analogues, helped to understand the critical moieties required for HO-2 activation. Vitamin K 3 57-66 heme oxygenase 2 Homo sapiens 134-138 31498618-8 2019 The subsequent reaction of most favourable diuron radical intermediate with other atmospheric reactive species, such as O2, HO2 and NOx (x =1, 2) radicals are studied. diuron radical 43-57 heme oxygenase 2 Homo sapiens 124-127