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- W2977505783 abstract "Abstract Electron and proton transfer reactions in enzymes are enigmatic and have attracted a great deal of theoretical, experimental, and practical attention. The oxidoreductases provide model systems for testing theoretical predictions, applying experimental techniques to gain insight into catalytic mechanisms, and creating industrially important bio(electro)conversion processes. Most previous and ongoing research on enzymatic electron transfer has exploited a theoretically and practically sound but limited approach that uses a series of structurally similar (“homologous”) substrates, measures reaction rate constants and Gibbs free energies of reactions, and analyses trends predicted by electron transfer theory. This approach, proposed half a century ago, is based on a hitherto unproved hypothesis that pre-exponential factors of rate constants are similar for homologous substrates. Here, we propose a novel approach to investigating electron and proton transfer catalysed by oxidoreductases. We demonstrate the validity of this new approach for elucidating the kinetics of oxidation of “non-homologous” substrates catalysed by compound II of Coprinopsis cinerea and Armoracia rusticana peroxidases. This study – using the Marcus theory – demonstrates that reactions are not only limited by electron transfer, but a proton is transferred after the electron transfer event and thus both events control the reaction rate of peroxidase-catalysed oxidation of substrates." @default.
- W2977505783 created "2019-10-10" @default.
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- W2977505783 date "2019-10-01" @default.
- W2977505783 modified "2023-10-12" @default.
- W2977505783 title "Consecutive Marcus Electron and Proton Transfer in Heme Peroxidase Compound II-Catalysed Oxidation Revealed by Arrhenius Plots" @default.
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- W2977505783 doi "https://doi.org/10.1038/s41598-019-50466-9" @default.
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- W2977505783 hasPublicationYear "2019" @default.
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