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lüll Observations concerning the quinol oxidation site of the cytochrome bc1 complex Berry EA; Huang LSFEBS Lett 2003[Nov]; 555 (1): 13-20A 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, electron paramagnetic resonance (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.|Animals[MESH]|Binding Sites[MESH]|Cattle[MESH]|Crystallography, X-Ray[MESH]|Electron Spin Resonance Spectroscopy[MESH]|Electron Transport[MESH]|Electron Transport Complex III/antagonists & inhibitors/*chemistry/metabolism[MESH]|Histidine/chemistry[MESH]|Hydrogen Bonding[MESH]|Hydroquinones/chemistry[MESH]|In Vitro Techniques[MESH]|Models, Molecular[MESH]|Oxidation-Reduction[MESH]|Protein Conformation[MESH]|Static Electricity[MESH] |