Circular dichroic evidence for a conformational change in a cytochrome b--c1 complex by uncoupling agents.
Circular dichroic spectra of the cytochrome b--c1 complex exhibit bilobe formation typical of exciton splitting in the presence of uncoupler. Bilobe formation occurs if both cytochrome c1 and cytochrome b are fully reduced. The fully oxidized and ascorbate-reduced complexes are not altered dichroically by uncouplers. The exciton splitting induced by uncoupler is consistent with heme--heme interaction: specifically, interaction between the two cytochromes b in the complex.
D002942:Circular Dichroism; D003574:Cytochrome c Group / Q000031:analogs & derivatives; D003580:Cytochromes; D003575:Cytochromes c1; D004227:Dithionite; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013053:Spectrophotometry; D014475:Uncoupling Agents
D003574:Cytochrome c Group; D003580:Cytochromes; D014475:Uncoupling Agents; D004227:Dithionite; D003575:Cytochromes c1