This chapter provides information on the purification and subunit composition of cytochrome c1 from bakers' yeast Saccharomyces cerevisiae. The purification of yeast cytochrome c, has allowed the study of its synthesis and incorporation into the inner mitochondrial membrane and initial studies of its structure with relationship to the rest of the cytochrome b-c1 complex. This procedure for the purification of yeast cytochrome cl yields a product with a heme cl content equal to or greater than that obtained with the analogous cytochrome from bovine heart. Yeast cytochrome c1 is reduced by dithionite or ascorbate and oxidized by ferricyanide, persulfate, or hydrogen peroxide. It is isolated in the reduced form; the reduced form does not react with oxygen, nor does it bind with carbon monoxide. This suggests that the environment of the heme group is not grossly altered relative to the membrane-bound cytochrome. Yeast cytochrome c1 is stable at 0°–4° in neutral buffer for several months, as determined by lack of spectral change and lack of autoxidizability.
ASJC Scopus subject areas
- Molecular Biology