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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 |
|---|---|
| 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
|
| Schlagwörter: |
| author_facet |
Khademian, Maryam Imlay, James A. Khademian, Maryam Imlay, James A. |
|---|---|
| author |
Khademian, Maryam Imlay, James A. |
| spellingShingle |
Khademian, Maryam Imlay, James A. Proceedings of the National Academy of Sciences Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor Multidisciplinary |
| author_sort |
khademian, maryam |
| spelling |
Khademian, Maryam Imlay, James A. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1701587114 <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> <i>Escherichia coli</i> cytochrome <i>c</i> peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor Proceedings of the National Academy of Sciences |
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| title |
Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_unstemmed |
Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_full |
Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_fullStr |
Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_full_unstemmed |
Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_short |
Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_sort |
<i>escherichia coli</i>
cytochrome
<i>c</i>
peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.1701587114 |
| publishDate |
2017 |
| physical |
|
| description |
<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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| author | Khademian, Maryam, Imlay, James A. |
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| author_sort | khademian, maryam |
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| description | <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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| spelling | Khademian, Maryam Imlay, James A. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1701587114 <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> <i>Escherichia coli</i> cytochrome <i>c</i> peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor Proceedings of the National Academy of Sciences |
| spellingShingle | Khademian, Maryam, Imlay, James A., Proceedings of the National Academy of Sciences, Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor, Multidisciplinary |
| title | Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_full | Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_fullStr | Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_full_unstemmed | Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_short | Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_sort | <i>escherichia coli</i> cytochrome <i>c</i> peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| title_unstemmed | Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1701587114 |