Observations concerning the quinol oxidation site of the cytochrome bc1 complex.
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, 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.
Berry
Edward A
EA
MS 64R121, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. eaberry@lbl.gov
Huang
Li-shar
LS
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D014450:Electron Transport Complex III / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D006639:Histidine / Q000737:chemistry; D006860:Hydrogen Bonding; D006873:Hydroquinones / Q000737:chemistry; D066298:In Vitro Techniques; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D055672:Static Electricity
D006873:Hydroquinones; D006639:Histidine; D014450:Electron Transport Complex III