Comparative study of the peptide composition of Complex III (quinol-cytochrome c reductase).

A comparative study has been made on the subunits of Complex III from beef heart, rat liver, Neurospora, and baker's yeast mitochondria. All of the subunits of the beef heart enzyme were similar to the counterpart subunit in rat liver Complex III, both with respect to their apparent molecular weights on SDS-polyacrylamide gels and their proteolytic digestion maps obtained in the presence of S. subtilus V8 protease. In contrast, the subunits of Neurospora and yeast Complex III varied considerably from the mammalian enzyme, as well as between themselves, the only exception being cytochrome b (subunit III). Less variation was observed in the electron transport peptides (IV-V) of higher and lower eukaryotes than in those subunits (I, II, VI-VIII) for which no functions are known. However, the data imply that subunits I, II, and VI-VIII are bona fide members of the complex, and that their functions within the complex, although unknown, are also somewhat conserved. Finally, the low-molecular-weight subunits of rat liver cytochrome oxidase and Complex III were compared. They appear to contain no subunits in common, implying different roles for these peptides in the two complexes.