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Observations concerning the quinol oxidation site of the cytochrome bc 1 complex
Author(s) -
Berry Edward A.,
Huang Li-shar
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01099-8
Subject(s) - chemistry , electron paramagnetic resonance , ubiquinol , electron transfer , electron transport chain , cluster (spacecraft) , crystallography , ligand (biochemistry) , ectodomain , iron–sulfur cluster , cytochrome , histidine , photochemistry , stereochemistry , coenzyme q – cytochrome c reductase , cytochrome c , nuclear magnetic resonance , physics , biochemistry , enzyme , mitochondrion , receptor , computer science , programming language
A direct hydrogen bond between ubiquinone/quinol bound at the Q O 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 bc 1 complex.