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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

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Publisher copy:
10.1021/acs.biochem.6b00868

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
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More from this funder
Funding agency for:
Armstrong, F
Grant:
BB/ I022309-1; BB/L009722/1
More from this funder
Funding agency for:
Islam, S
Grant:
Merit Scholarship Programme for High Technology
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
Source identifiers:
667799
Language:
English
Pubs id:
pubs:667799
UUID:
uuid:3f7e03d1-6c2b-4390-b001-524bb656625a
Local pid:
pubs:667799
Deposit date:
2017-01-06

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