Journal article
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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- Files:
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(Accepted manuscript, pdf, 669.7KB)
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- Publisher copy:
- 10.1021/acs.analchem.6b03589
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Authors
Funding
+ Biotechnology and Biological Sciences Research Council
More from this funder
Funding agency for:
Adamson, H
Grant:
BB/F017316/1
+ Engineering and Physical Sciences Research Council
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Funding agency for:
Robinson, M
Grant:
EP/I017909/1
+ Deutsche Forschungsgemeinschaft
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Funding agency for:
Soboh, B
Grant:
SO 1325/5-1
+ Royal Society
More from this funder
Funding agency for:
Simonov, A
Grant:
International Exchange Scheme
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Bibliographic Details
- 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
Item Description
- Pubs id:
-
pubs:668668
- UUID:
-
uuid:7232e4e4-d940-4f18-86a5-491779c95251
- Local pid:
- pubs:668668
- Deposit date:
- 2017-01-09
Terms of use
- Copyright holder:
- © 2016 American Chemical Society
- Copyright date:
- 2016
- Notes:
- This is the author accepted manuscript following peer review version of the article. The final version is available online from Elsevier at: 10.1021/acs.analchem.6b03589
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