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• W2169662276 abstract "An oxygen-tolerant respiratory [NiFe]-hydrogenase is proven to be a four-electron hydrogen/oxygen oxidoreductase, catalyzing the reaction 2 H2 + O2 = 2 H2O, equivalent to hydrogen combustion, over a sustained period without inactivating. At least 86% of the H2O produced by Escherichia coli hydrogenase-1 exposed to a mixture of 90% H2 and 10% O2 is accounted for by a direct four-electron pathway, whereas up to 14% arises from slower side reactions proceeding via superoxide and hydrogen peroxide. The direct pathway is assigned to O2 reduction at the [NiFe] active site, whereas the side reactions are an unavoidable consequence of the presence of low-potential relay centers that release electrons derived from H2 oxidation. The oxidase activity is too slow to be useful in removing O2 from the bacterial periplasm; instead, the four-electron reduction of molecular oxygen to harmless water ensures that the active site survives to catalyze sustained hydrogen oxidation." @default.
• W2169662276 created "2016-06-24" @default.
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• W2169662276 date "2014-04-08" @default.
• W2169662276 modified "2023-10-13" @default.
• W2169662276 title "How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases" @default.
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• W2169662276 doi "https://doi.org/10.1073/pnas.1322393111" @default.
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• W2169662276 hasPublicationYear "2014" @default.
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