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Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
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| Personen und Körperschaften: | , |
| In: | Proceedings of the National Academy of Sciences, 114, 2017, 33 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| Zusammenfassung: | <jats:title>Significance</jats:title> <jats:p> Hydrogen peroxide has been regarded exclusively as a hazard for bacteria; its sources and concentrations in natural habitats are uncertain. The cytochrome <jats:italic>c</jats:italic> peroxidase of <jats:italic>Escherichia coli</jats:italic> exhibits an expression pattern and flux rate that provides surprising insights into these issues. This periplasmic enzyme is induced only when H <jats:sub>2</jats:sub> O <jats:sub>2</jats:sub> is present and molecular oxygen is absent. Intriguingly, it was ineffective as a defensive enzyme, but through its linkage to the quinone pool it did enable <jats:italic>E. coli</jats:italic> to respire using H <jats:sub>2</jats:sub> O <jats:sub>2</jats:sub> as an anaerobic electron acceptor. We suggest that both chemical and biotic processes generate micromolar H <jats:sub>2</jats:sub> O <jats:sub>2</jats:sub> at oxic/anoxic interfaces and that this scenario is common enough that microbes have evolved strategies to productively exploit the H <jats:sub>2</jats:sub> O <jats:sub>2</jats:sub> . </jats:p> |
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| ISSN: |
0027-8424
1091-6490 |
| DOI: | 10.1073/pnas.1701587114 |