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Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance

Abstract:

In oxidative phosphorylation, complex I (NADH:quinone oxidoreductase) couples electron transfer to proton translocation across an energy-transducing membrane. Complex I contains a flavin mononucleotide to oxidize NADH, and an unusually long series of iron-sulfur (FeS) clusters, in several subunits, to transfer the electrons to quinone. Understanding coupled electron transfer in complex I requires a detailed knowledge of the properties of individual clusters and of the cluster ensemble, and so...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1073/pnas.0908050107

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
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Institution:
Medical Research Council Mitochondrial Biology Unit, Wellcome Trust/Medical Research Council Building, Cambridge, UK
Role:
Author
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Institution:
Medical Research Council Mitochondrial Biology Unit, Wellcome Trust/Medical Research Council Building, Cambridge, UK
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
Department:
Mathematical,Physical & Life Sciences Division - Chemistry - Center for Advanced Electron Spin Resonance
Role:
Author
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Medical Research Council More from this funder
Engineering and Physical Sciences Research Council More from this funder
Publisher:
National Academy of Sciences Publisher's website
Journal:
Proceedings of the National Academy of Sciences Journal website
Volume:
107
Issue:
5
Pages:
1930-1935
Publication date:
2010-02-01
DOI:
EISSN:
1091-6490
Language:
English
Keywords:
Subjects:
UUID:
uuid:3fd6173a-4155-446d-b371-daf5a3f2f966
Local pid:
ora:5602
Deposit date:
2011-07-21

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