Volbeda, Anne, Mouesca, Jean-Marie, Darnault, Claudine et al. (4 more authors) (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. pp. 7175-7178. ISSN 1364-548X
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 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. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 03 Sep 2018 16:30 |
Last Modified: | 16 Oct 2024 15:02 |
Published Version: | https://doi.org/10.1039/c8cc02896f |
Status: | Published online |
Refereed: | Yes |
Identification Number: | 10.1039/c8cc02896f |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:135260 |