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Synchrotron-based Infrared Microanalysis of Biological Redox Processes under Electrochemical Control

Abstract:

We describe a method for addressing redox enzymes adsorbed on a carbon electrode using synchrotron infrared microspectroscopy combined with protein film electrochemistry. Redox enzymes have high turnover frequencies, typically 10-1000 s-1, and therefore fast experimental triggers are needed in order to study sub-turnover kinetics and identify the involvement of transient species important to their catalytic mechanism. In an electrochemical experiment this equates to the use of microelectrodes...

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Publication status:
Published
Peer review status:
Peer reviewed

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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
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
More from this funder
Name:
Oxford Clarendon Fund
Funding agency for:
Chung, M
Grant:
Scholarship
More from this funder
Name:
European Molecular Biology Organization
Funding agency for:
Reeve, H
Grant:
Postdoctoral fellowship
More from this funder
Name:
Engineering and Physical Sciences Research Council
Funding agency for:
Quinson, J
Lonsdale, T
Grant:
EP/J500495/1
EP/L505031/1
EP/K031503/1; INSPIRE award EP/J015202/1
More from this funder
Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/L009722/1
More from this funder
Name:
European Research Council
Grant:
EnergyBioCatalysis-ERC-2010-StG-258600
Publisher:
ACS
Journal:
Analytical Chemistry More from this journal
Publication date:
2016-06-07
Acceptance date:
2016-06-07
ISSN:
1086-4377
Pubs id:
pubs:626337
UUID:
uuid:6f4b0fc2-e00b-45bd-8de1-a4a9baa40c63
Local pid:
pubs:626337
Source identifiers:
626337
Deposit date:
2016-06-07

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