The effect of complete or specific partial acetimidylation on the biological properties of cytochrome c and cytochrome c-T.
The biological consequences of acetimidylation of all 19 epsilon-amino groups of horse cytochrome c are a slight decrease in both the redox potential of the protein and its ability to stimulate oxygen uptake in the cytochrome c-depleted-mitochondria assay. Examination of a number of specific partially acetimidylated analogues and acetimidylated cytochromes c of other species has shown that the changes in biological properties, which are associated with a slight structural change as monitored by n.m.r. spectroscopy [Boswell, Moore, Williams, Harris, Wallace, Bocieck & Welti (1983) Biochem. J. 213, 679-686], appear to stem from modification of residues in a restricted region of the sequence. The failure of the redox potential of Saccharomyces cerevisae cytochrome c to be affected by acetimidylation suggests that it is lysine-53, absent from that species, that is the sensitive residue.
D000818:Animals; D001665:Binding Sites; D002175:Candida / Q000032:analysis; D002678:Chimera; D003574:Cytochrome c Group / Q000031:analogs & derivatives* / Q000378:metabolism*; D045304:Cytochromes c; D006736:Horses; D008929:Mitochondria, Heart / Q000378:metabolism; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000032:analysis
D003574:Cytochrome c Group; D010446:Peptide Fragments; C040819:cytochrome c, N-epsilon-acetimidate; D045304:Cytochromes c; C040820:cytochrome c-T