Open AccessThe Cytochrome bc 1 Complex of Yeast Mitochondria
Author(s) -
KATAN Martijn B.,
POOL Loes,
GROOT Gert S. P.
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10393.x
Subject(s) - coenzyme q – cytochrome c reductase , cytochrome c1 , cytochrome , gel electrophoresis , chemistry , cytochrome b , cytochrome c , heme , amino acid , hemeprotein , polyacrylamide gel electrophoresis , biochemistry , sodium , guanidine , cytochrome c peroxidase , mitochondrion , enzyme , organic chemistry , mitochondrial dna , gene
We have isolated the cytochrome bc 1 complex and some of its constituent polypeptides from baker's yeast and have studied its properties by spectroscopy, electrophoresis and amino acid analysis The isolated complex contained 6 μmol of b heme and approximately 3 μmol of c 1 heme per g of protein. The electron paramagnetic resonance spectrum was similar to that of the beef‐heart preparation. The complex consisted of 7 polypeptides with mobilities on sodium dodecylsulphate polyacrylamide gel electrophoresis corresponding to Mr 44000, 40000, 32000, 32000, 17000, 14000 and 11000. One of the polypeptides with Mr 32000 was identified on sodium dodecylsulphate gels as cytochrome c 1 by porphyrin fluorescence. Cytochrome b was isolated from the complex by treating it with guanidine hydrochloride; it had a purity of 20 μmot per g of protein and consisted of a polypeptide with Mr 32000 plus two minor bands with Mr 14000 and 11000. We have isolated the polypeptide of Mr 32000 from cytochrome b and the polypeptides of Mr 44000 and 40000 (“core proteins”) from the complex, both by preparative sodium dodecylsulphate gel electrophoresis and determined their amino acid composition. Only the b polypeptide of Mr 32000 shows the low proportion of polar amino acid residues that is considered typical of membrane proteins.