Cm. Cruciat et al., The cytochrome bc(1) and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria, J BIOL CHEM, 275(24), 2000, pp. 18093-18098
The mitochondrial electron transport chain complexes are large multisubunit
complexes embedded in the inner membrane. We report here that in the yeast
Saccharomyces cerevisiae, the cytochrome be, and cytochrome c oxidase comp
lexes co-exist as a larger complex of similar to 1000 kDa in the mitochondr
ial membrane. Following solubilization with a mild detergent, the cytochrom
e bc(1)-cytochrome c oxidase complex remains stable. It was analyzed using
the techniques of gel filtration and blue native-polyacrylamide gel electro
phoresis. Direct physical. association of subunits of the cytochrome be, co
mplex with those of the cytochrome c oxidase complex was verified by co-imm
unoprecipitation analysis. Our data indicate that the cytochrome be, comple
x is exclusively in association with the cytochrome c oxidase complex in ye
ast mitochondria. We term this complex the cytochrome bc(1)-cytochrome c ox
idase supracomplex.