X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster

Anne Volbeda; Jean-Marie Mouesca; Claudine Darnault; Maxie M. Roessler; Alison Parkin; Fraser A Armstrong; Juan C Fontecilla-Camps

doi:10.1039/c8cc02896f

X-ray structural, functional and computational studies of the O₂-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster

Anne Volbeda, Jean-Marie Mouesca, Claudine Darnault, Maxie M. Roessler, Alison Parkin, Fraser A Armstrong, Juan C Fontecilla-Camps

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The crystal structure of the Escherichia coli O₂-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O₂-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O₂ sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.

Original language	English
Pages (from-to)	7175-7178
Number of pages	4
Journal	Chemical Communications
Volume	54
Early online date	5 Jun 2018
DOIs	https://doi.org/10.1039/c8cc02896f
Publication status	E-pub ahead of print - 5 Jun 2018

Bibliographical note

© The Royal Society of Chemistry 2018. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

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10.1039/c8cc02896f

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© The Royal Society of Chemistry 2018. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.
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Cite this

Volbeda, A., Mouesca, J.-M., Darnault, C., Roessler, M. M., Parkin, A., Armstrong, F. A., & Fontecilla-Camps, J. C. (2018). X-ray structural, functional and computational studies of the O₂-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster. Chemical Communications, 54, 7175-7178. Advance online publication. https://doi.org/10.1039/c8cc02896f

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abstract = "The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.",

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AU - Mouesca, Jean-Marie

AU - Darnault, Claudine

AU - Roessler, Maxie M.

AU - Parkin, Alison

AU - Armstrong, Fraser A

AU - Fontecilla-Camps, Juan C

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N2 - The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.

AB - The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.

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