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A cytochrome c1 subcomplex was obtained from purified complex III. The subcomplex consists of three protein subunits, present at an equimolar stoichiometry. The primary structures of two of these proteins, the heme-carrying cytochrome c1 and a protein with a molecular mass of 9175 Da, have been published by Wakabayashi et al. The covalent structure of the smallest subunit is presented in this paper. This protein consists of 62 amino acid residues; its molecular mass was calculated to be 7189 Da. The sequence was determined by complete solid-phase Edman degradation of the uncleaved polypeptide and was confirmed by sequencing the C-terminal fragment resulting from cleavage of a single tryptophyl bond.
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