PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 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 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 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 27465104-7 2016 abstracts hydrogen rapidly from H2 O2 to produce HO2 (.) Hydrogen 10-18 heme oxygenase 2 Homo sapiens 49-52 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 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 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 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 29533404-4 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 29533404-7 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. Hydrogen 160-168 heme oxygenase 2 Homo sapiens 204-207 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 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 27164019-1 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 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 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 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 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 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 25988324-1 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 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 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 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 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 23822586-0 2013 Hydrogen abstraction from n-butyl formate by H and HO2 . Hydrogen 0-8 heme oxygenase 2 Homo sapiens 52-55 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 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 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 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 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 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 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 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 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 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 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 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 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 16366658-1 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 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 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 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