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Hydrogen activation by [NiFe]-hydrogenases

Abstract:

Hydrogenase-1 (Hyd-1) from Escherichia coli is a membrane-bound enzyme that catalyses the reversible oxidation of molecular H2 The active site contains one Fe and one Ni atom and several conserved amino acids including an arginine (Arg(509)), which interacts with two conserved aspartate residues (Asp(118) and Asp(574)) forming an outer shell canopy over the metals. There is also a highly conserved glutamate (Glu(28)) positioned on the opposite side of the active site to the canopy. The mechan...

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

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Publisher copy:
10.1042/BST20160031

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
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Funding agency for:
Armstrong, FA
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Funding agency for:
Phillips, SE
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Publisher:
Portland Press Publisher's website
Journal:
Biochemical Society transactions Journal website
Volume:
44
Issue:
3
Publication date:
2016-01-01
DOI:
EISSN:
1470-8752
ISSN:
0300-5127
URN:
uuid:77efd9fa-a1d7-4fe5-8663-9585c2e6050a
Source identifiers:
628815
Local pid:
pubs:628815
Paper number:
3

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