Resolution of the circular dichroism spectra of the mitochondrial cytochrome bc1 complex.
The circular dichroic spectrum of the mitochondrial cytochrome bc1 complex isolated from bovine heart has been resolved into the contributions from the prosthetic groups: cytochrome c1, the 'Rieske' iron-sulphur centre and the two b cytochromes. It is apparent that firstly, the circular dichroism (CD) properties of cytochrome c1 within the bc1 complex differ from those found in the isolated cytochrome c1 and secondly, both the oxidized and reduced b cytochromes exhibit an intense spectrum of bilobic shape, with the wavelengths of the cross-over points closely corresponding to those of the maxima in the optical absorbance spectra. These latter CD features are discussed in relation to the proposed structure of cytochrome b.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003573:Cytochrome b Group / Q000302:isolation & purification; D003575:Cytochromes c1 / Q000302:isolation & purification; D014450:Electron Transport Complex III / Q000302:isolation & purification*; D007506:Iron-Sulfur Proteins / Q000302:isolation & purification; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction
D003573:Cytochrome b Group; D007506:Iron-Sulfur Proteins; D003575:Cytochromes c1; D014450:Electron Transport Complex III