Observations concerning the quinol oxidation site of the cytochrome bc{sub 1} complex
Journal Article
·
· Federation of European Biochemical Societies
A direct hydrogen bond between ubiquinone/quinol bound at the QO site and a cluster-ligand histidine of the iron-sulfur protein (ISP) is described as a major determining factor explaining much experimental data on position of the ISP ectodomain, EPR lineshape and midpoint potential of the iron-sulfur cluster, and the mechanism of the bifurcated electron transfer from ubiquinol to the high and low potential chains of the bc1 complex.
- Research Organization:
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Sponsoring Organization:
- USDOE; National Institute of Health Grant DK44842 (US)
- DOE Contract Number:
- AC03-76SF00098
- OSTI ID:
- 832755
- Report Number(s):
- LBNL-53853; R&D Project: 864U1D; TRN: US200429%%1555
- Journal Information:
- Federation of European Biochemical Societies, Vol. 555, Issue 1; Other Information: Journal Publication Date: 11/27/2003; PBD: 7 Sep 2003
- Country of Publication:
- United States
- Language:
- English
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