期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 18, 页码 6606-6611出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1322393111
关键词
hydrogen; mass spectrometry; Fe-S cluster
资金
- Biological and Biotechnological Sciences Research Council [BB/H003878-1, BB/I022309-1, BB/H001190/1, BB/I02008X/1]
- St John's College, Oxford
- Royal Society
- BBSRC [BB/L008521/1, BB/H001190/1, BB/I02008X/1, BB/I022309/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I02008X/1, BB/I022309/1, BB/L008521/1, BB/H001190/1] Funding Source: researchfish
An oxygen-tolerant respiratory [NiFe]-hydrogenase is proven to be a four-electron hydrogen/oxygen oxidoreductase, catalyzing the reaction 2 H-2 + O-2 = 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% H-2 and 10% O-2 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 O-2 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 H-2 oxidation. The oxidase activity is too slow to be useful in removing O-2 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.
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