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- W2080341639 abstract "A recent report by Mills and Klinman [Mills, S. A., and Klinman, J. P. (2000) J. Am. Chem. Soc. 122, 9897−9904] described the preparation and initial characterization of a cobalt-substituted form of the copper amine oxidase from Hansenula polymorpha (HPAO). This enzyme was found to be fully catalytically active at saturating substrate concentrations, but with a Km for O2 approximately 70-fold higher than that of the copper-containing, wild-type enzyme. Herein, we report a detailed analysis of the mechanism of catalysis for the wild-type and the cobalt-substituted forms of HPAO. Both forms of enzyme are concluded to utilize the same mechanism for oxygen reduction, involving initial, rate-limiting electron transfer from the reduced cofactor of the enzyme to prebound dioxygen. Superoxide formed in this manner is stabilized by the active site metal, facilitating the transfer of a second electron and two protons to form the product hydrogen peroxide. The elevated Km for O2 at the dioxygen binding site in Co-substituted HPAO, relative to that of wild-type HPAO, is proposed to be due to a change in the net charge at the adjacent metal site from +1 (cupric hydroxide) in wild-type enzyme to +2 (cobaltous H2O) in cobalt-substituted HPAO." @default.
- W2080341639 created "2016-06-24" @default.
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- W2080341639 date "2002-07-30" @default.
- W2080341639 modified "2023-10-16" @default.
- W2080341639 title "Mechanistic Comparison of the Cobalt-Substituted and Wild-Type Copper Amine Oxidase from <i>Hansenula polymorpha</i>" @default.
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- W2080341639 doi "https://doi.org/10.1021/bi0200864" @default.
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