Circular-dichroism studies of the cytochrome b-c1 complex of Saccharomyces cerevisiae.
1. Circular dichroism studies on the Soret region of the cytochrome b-c1 complex of yeast reveal a change in the dichroism of cytochrome c1 depending on the redox state of cytochrome b, indicating a conformational interaction between both cytochromes. 2. This interaction is not influenced by binding of the inhibitor antimycin A to the complex, so that the interaction does not appear to be involved in the mechanism of electron transport through the complex. 3. Antimycin A binding causes a complex set of changes in the CD spectrum of the complex, which can be attributed to a severe and specific distortion of the environment of the chromophore of cytochrome b.
D000968:Antimycin A; 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*
D003574:Cytochrome c Group; D003580:Cytochromes; D004227:Dithionite; D000968:Antimycin A; D003575:Cytochromes c1