Journal article
Importance of the active site "canopy" residues in an O2-tolerant [NiFe]-hydrogenase
- Abstract:
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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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- Files:
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(Accepted manuscript, pdf, 1004.0KB)
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- Publisher copy:
- 10.1021/acs.biochem.6b00868
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Authors
Funding
+ Engineering and Physical Sciences
Research Council
More from this funder
Funding agency for:
Brooke, E
+ Biological and
Biotechnology Sciences Research Council
More from this funder
Funding agency for:
Armstrong, F
Grant:
BB/
I022309-1; BB/L009722/1
+ Islamic Development Bank
More from this funder
Funding agency for:
Islam, S
Grant:
Merit Scholarship Programme
for High Technology
+ Biological and
Biotechnology Sciences Research Council
More from this funder
Grant:
BB/
I022309-1 and BB/L009722/1 to F.A.A.
Bibliographic Details
- 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
Item Description
- Language:
- English
- Pubs id:
-
pubs:667799
- UUID:
-
uuid:3f7e03d1-6c2b-4390-b001-524bb656625a
- Local pid:
- pubs:667799
- Deposit date:
- 2017-01-06
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2016
- Notes:
- Copyright © 2016 American Chemical Society. This is the accepted manuscript version of the article. The final version is available online from the American Chemical Society at: https://doi.org/10.1021/acs.biochem.6b00868
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