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How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Wulff, Philip Day, Christopher C. Sargent, Frank Armstrong, Fraser A. |
| Copyright Year | 2014 |
| 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. |
| File Format | PDF HTM / HTML |
| DOI | 10.1073/pnas.1322393111 |
| PubMed reference number | 24715724 |
| Journal | Medline |
| Volume Number | 111 |
| Issue Number | 18 |
| Alternate Webpage(s) | http://www.pnas.org/content/111/18/6606.full.pdf |
| Alternate Webpage(s) | https://doi.org/10.1073/pnas.1322393111 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
