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

Journal article

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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Authors: Roessler, M; King, MS; Robinson, A; Armstrong, F; Harmer, J

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 107
• Issue: 5
• Pages: 1930-1935
• Publication date: 2010-02-01
• DOI: 10.1073/pnas.0908050107
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Cattle; Models, Molecular; Electron Spin Resonance Spectroscopy; Thermus thermophilus; Electron Transport Complex I; Bacterial Proteins; Molecular Structure; Protein Structure, Tertiary; Animals; Electron Transport; Energy Transfer