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Importance of the active site "canopy" residues in an O2-tolerant [NiFe]-hydrogenase

Abstract:

The active site of Hyd-1, an oxygen-tolerant membrane-bound [NiFe]-hydrogenase from Escherichia coli, contains four highly conserved residues that form a "canopy" above the bimetallic center, closest to the site at which exogenous agents CO and O2 interact, substrate H2 binds, and a hydrido intermediate is stabilized. Genetic modification of the Hyd-1 canopy has allowed the first systematic and detailed kinetic and structural investigation of the influence of the immediate outer coordination ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

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Publisher copy:
10.1021/acs.biochem.6b00868

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Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Author
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Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Author
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Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
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Publisher:
American Chemical Society Publisher's website
Journal:
Biochemistry Journal website
Volume:
56
Issue:
1
Pages:
132–142
Publication date:
2016-12-21
Acceptance date:
2016-12-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Pubs id:
pubs:667799
URN:
uri:3f7e03d1-6c2b-4390-b001-524bb656625a
UUID:
uuid:3f7e03d1-6c2b-4390-b001-524bb656625a
Local pid:
pubs:667799
Paper number:
1
Language:
English

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