Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase.
The EPR spectra of the cytochromes in ubiquinol-cytochrome c oxidoreductase (Complex III) have peaks at g = 3.78 (cytochrome b566) g = 3.45 (cytochrome b562) and g = 3.35 (cytochrome c1). The highly asymmetric peak of cytochrome b566 has been simulated using an arbitrary gaussian distribution of crystal field parameters. The asymmetry is due to the nonlinear relationship between field position and crystal field. The results suggest that the b cytochromes have bis-imidazole ligation. The gz peak of cytochrome c1 was also found to be asymmetric; simulations suggest histidine-methionine ligation. No other important cytochrome components were needed to simulate the spectrum of the oxidized complex; these results are consistent with 1:1:1 stoichiometry of components. These results argue against any asymmetric dimer model for Complex III.
D003573:Cytochrome b Group / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism; D003580:Cytochromes / Q000378:metabolism*; D015786:Cytochromes b5; D004578:Electron Spin Resonance Spectroscopy; D014450:Electron Transport Complex III; D009097:Multienzyme Complexes / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D011808:Quinone Reductases / Q000378:metabolism*; D012984:Software
D003573:Cytochrome b Group; D003574:Cytochrome c Group; D003580:Cytochromes; D009097:Multienzyme Complexes; D015786:Cytochromes b5; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases; D014450:Electron Transport Complex III