[Role of individual lysine residues of horse cytochrome c in the formation of reactive complexes with components of the respiratory chain].
A number of mutant forms of horse cytochrome-c with single or double substitutions of lysine residues near the heme cavity was prepared that provided an interaction of mitochondrial ubiquinone with cytochrome-c reductase (EC 1.10.2.2) (complex III) and cytochrome-c oxidase (EC 1.9.3.1) (complex IV). The succinate cytochrome-c reductase and cytochrome-c oxidase activities of mitoplasts of rat liver were measured in the presence of mutant forms of cytochrome-c. The lysine residues in positions 8, 27, 72, 86, and 87 were shown to be the main contribution to the formation of a reactive complex with ubiquinol-cytochrome-c reductase of the respiratory chain, whereas the lysine residues in positions 13, 79, 86, and 87 were predominantly responsible for the formation of a complex with cytochrome-c oxidase.
Pepelina
T Iu
TIu
Chertkova
R V
RV
Dolgikh
D A
DA
Kirpichnikov
M P
MP
D019943:Amino Acid Substitution; D000818:Animals; D045304:Cytochromes c / Q000235:genetics / Q000378:metabolism*; D014450:Electron Transport Complex III / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000378:metabolism*; D006736:Horses; D007700:Kinetics; D008239:Lysine / Q000235:genetics*; D008930:Mitochondria, Liver / Q000201:enzymology; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D051381:Rats; D019802:Succinic Acid / Q000378:metabolism
D045304:Cytochromes c; D019802:Succinic Acid; D003576:Electron Transport Complex IV; D014450:Electron Transport Complex III; D008239:Lysine