PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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. Hydrogen Peroxide 71-75 heme oxygenase 2 Homo sapiens 154-157 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 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 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. 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 . Hydrogen Peroxide 113-117 heme oxygenase 2 Homo sapiens 172-175 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 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 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 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 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 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 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 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 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 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 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 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 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. Hydrogen Peroxide 256-260 heme oxygenase 2 Homo sapiens 199-202 27465104-7 2016 abstracts hydrogen rapidly from H2 O2 to produce HO2 (.) Hydrogen Peroxide 32-37 heme oxygenase 2 Homo sapiens 49-52 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 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 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 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 26633020-4 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 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 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. Hydrogen Peroxide 408-412 heme oxygenase 2 Homo sapiens 136-139 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 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 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 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 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 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 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 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 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 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 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 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 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 16366658-1 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 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 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 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 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 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 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 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 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 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 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 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 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 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 2492791-15 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 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 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 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