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- W1990233438 abstract "Chloroperoxidase is a versatile fungal heme-thiolate protein that catalyzes a variety of one-electron and two-electron oxidations. We report here that the alkylation of an essential histidine residue showed no effect on the one-electron peroxidations but inhibited two-electron oxidations. The pH profiles of different peroxidative substrates showed optimal activities at varying pH values for the same enzyme. 2-Allylphenol and substituted ortho-phenolics showed efficient peroxidations. Also, substrates excluded from the active site (or with no favorable positioning at the heme center or heme edge) were converted in the peroxidation reaction. While hydrogen peroxide serves as the superior activator in the two-electron oxidations, small alkylhydroperoxides give much better rates for peroxidation reactions. All the above observations indicate that one-electron oxidations are mechanistically quite different from the two-electron oxidations catalyzed by chloroperoxidase. We propose that the peroxidatic substrates interact predominantly outside the heme active site, presumably at the surface of the enzyme." @default.
- W1990233438 created "2016-06-24" @default.
- W1990233438 creator A5062465747 @default.
- W1990233438 creator A5063916487 @default.
- W1990233438 date "2008-01-26" @default.
- W1990233438 modified "2023-09-27" @default.
- W1990233438 title "Chloroperoxidase, a Janus Enzyme" @default.
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- W1990233438 doi "https://doi.org/10.1021/bi7022656" @default.
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