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Journal Article

Three molecules of ubiquinone bind specifically to mitochondrial cytochrome bc1 complex


Lancaster,  C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Bartoschek, S., Johansson, M., Geierstanger, B. H., Okun, j. G., Lancaster, C. R. D., Humpfer, E., et al. (2001). Three molecules of ubiquinone bind specifically to mitochondrial cytochrome bc1 complex. The Journal of Biological Chemistry, 276(38), 35231-35234. doi:10.1074/jbc.c100365200.

Cite as: https://hdl.handle.net/21.11116/0000-0007-0AEF-2
Bifurcated electron flow to high potential "Rieske" iron-sulfur cluster and low potential heme bL is crucial for respiratory energy conservation by the cytochrome bc1 complex. The chemistry of ubiquinol oxidation has to ensure the thermodynamically unfavorable electron transfer to heme bL. To resolve a central controversy about the number of ubiquinol molecules involved in this reaction, we used high resolution magic-angle-spinning nuclear magnetic resonance experiments to show that two out of three n-decyl-ubiquinones bind at the ubiquinol oxidation center of the complex. This substantiates a proposed mechanism in which a charge transfer between a ubiquinol/ubiquinone pair explains the bifurcation of electron flow.