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- W2073997906 abstract "The kinetics of the reactions of hydrogen peroxide and cyanide with native horseradish peroxidase, as well as reactions of compounds I and II with ferrocyanide have been studied in ordinary water and in deuterium oxide at 25 °C and ionic strength 0.11 using a stopped-flow apparatus. Rate constants for all reactions were measured over a wide range of acidity in both solvents from which equilibrium and kinetic isotope effects were evaluated. Protonation of an ionizable group on the enzyme with a pK a value of 4.15 ± 0.05 in water inhibits the reactions with both hydrogen peroxide and cyanide. A significant kinetic isotope effect, k H /k D = 1.6 ± 0.1, was measured for compound I formation whereas no significant kinetic isotope effect was found for cyanide binding. On the basis of these findings, a partial mechanism for compound I formation is proposed in which the group of pK a 4.15 plays a crucial role. The pH dependencies of the ferrocyanide reaction in the pH interval 4.5–10.8 confirmed the role of an acid group with a pK a of 5.2 for compound I and for compound II a pK a of 8.6 and another with a value lower than that encompassed by the pH range of the study. Equilibrium isotope effects were found but no kinetic isotope effects for either the reaction of compound I or of compound II This suggests that there are no rate-limiting proton transfers in the reactions between ferrocyanide and compounds I and II of horseradish peroxidase. The only reducing substrates which exhibit positive k H /k D values possess a labile proton." @default.
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- W2073997906 title "Horseradish peroxidase. XXIX. Reactions in water and deuterium oxide: cyanide binding, compound I formation, and reactions of compounds I and II with ferrocyanide" @default.
- W2073997906 doi "https://doi.org/10.1139/v78-468" @default.
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