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Analysis of HypD disulfide redox chemistry via optimization of fourier transformed ac voltammetric data

Abstract:

Rapid disulfide bond formation and cleavage is an essential mechanism of life. Using large amplitude Fourier transformed alternating current voltammetry (FTacV) we have measured previously uncharacterized disulfide bond redox chemistry in Escherichia coli HypD. This protein is representative of a class of assembly proteins that play an essential role in the biosynthesis of the active site of [NiFe]-hydrogenases, a family of H2-activating enzymes. Compared to conventional electrochemical metho...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/acs.analchem.6b03589

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Institution:
University of Oxford
Division:
MPLS
Department:
Computer Science
Role:
Author
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Institution:
University of Oxford
Division:
MPLS
Department:
Mathematical Institute
Role:
Author
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Funding agency for:
Adamson, H
Grant:
BB/F017316/1
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Funding agency for:
Robinson, M
Grant:
EP/I017909/1
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Funding agency for:
Soboh, B
Grant:
SO 1325/5-1
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Funding agency for:
Simonov, A
Grant:
International Exchange Scheme
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Publisher:
American Chemical Society Publisher's website
Journal:
Analytical Chemistry Journal website
Volume:
89
Issue:
3
Pages:
1565–1573
Publication date:
2016-12-28
Acceptance date:
2016-12-18
DOI:
EISSN:
1520-6882
ISSN:
0003-2700
Source identifiers:
668668
Pubs id:
pubs:668668
UUID:
uuid:7232e4e4-d940-4f18-86a5-491779c95251
Local pid:
pubs:668668
Deposit date:
2017-01-09

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