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

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 re...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1039/c8cc02896f

Authors


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ORCID:
0000-0002-6038-0979
Mouesca, JM More by this author
Darnault, C More by this author
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ORCID:
0000-0002-5291-4328
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ORCID:
0000-0003-4715-7200
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Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Communications Journal website
Volume:
52
Issue:
54
Pages:
7175-7178
Publication date:
2018-06-05
Acceptance date:
2018-06-04
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
Pubs id:
pubs:857562
URN:
uri:e5b6985c-a65d-4cfb-8345-e430c3897fc8
UUID:
uuid:e5b6985c-a65d-4cfb-8345-e430c3897fc8
Local pid:
pubs:857562

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