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- W2078643598 abstract "Reaction of horseradish peroxidase A2 and C with superoxide anion (O2−) has been studied using pulse radiolysis technique. Peroxidase C formed Compound I and an oxy form of the enzyme due to reaction of ferric enzyme with hydrogen peroxide (H2O2) and O2−, respectively. At low concentrations of O2− (<1 μM), O2− reacted with ferric peroxidase C nearly quantitatively and formation of H2O2 was negligible. The rate constant for the reaction was found to be increased below pH 6 and this phenomenon can be explained by assuming that HO2 reacts with peroxidase C more rapidly than O2−. In contrast, the formation of oxyperoxidase could not be detected in the case of peroxidase A2 after the pulse, and only Compound I of the enzyme was formed. Peroxidase A2, however, produced the oxy form upon aerobic addition of NADH, suggesting that O2− can also react with peroxidase A2 to form the oxy form. The results at present indicate that the rate constant for the reaction of O2− with peroxidase A2 is smaller than 103 M−1·s−1." @default.
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- W2078643598 date "1989-04-01" @default.
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- W2078643598 title "Kinetics of the reaction of superoxide anion with ferric horseradish peroxidase" @default.
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- W2078643598 doi "https://doi.org/10.1016/0167-4838(89)90071-x" @default.
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