Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc1, and cytochrome c1. Differential acetylation of lysyl residues in free and complexed cytochrome c.

摘要: The isolated complexes of ferricytochrome c with cytochrome oxidase, reductase (cytochrome bc1 or complex III), and c1 (a subunit reductase) were investigated by the method differential chemical modification (Bosshard, H.R. (1979) Methods Biochem. Anal. 25, 273-301). By this reactivity each 19 lysyl side chains horse was compared in free complexed binding sites deduced from altered reactivities particular c. most important findings follow. 1. on for oxidase reductase, defined terms involvement residues, are indistinguishable. two oxidation-reduction partners interact at front (exposed heme edge) top left part molecule, shielding mainly residues 8, 13, 72 + 73, 86, 87. 22, 39, 53, 55, 60, 99, 100 is unaffected formation while remaining positions 5, 7, 27, 79, 88 somewhat less reactive molecule. 2. When bound to same shielded. This indicates that binds during electron transfer process.