PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 17455918-11 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. 7 alpha-hydroxy-4-cholesten-3-one 126-129 heme oxygenase 2 Homo sapiens 25-28