Binding of arylazidocytochrome c to yeast cytochrome c peroxidase.
Cytochrome c derivatives modified with a photoactivatable arylazido group in selected lysine residues were irradiated in the presence of cytochrome c peroxidase (EC 1.11.1.5). A derivative modified at lysine 13 was able to cross-link to the enzyme and inhibit electron transfer activity. Complete inhibition of cytochrome c peroxidase activity was obtained when 1 mol of cytochrome c was covalently bound per mol of cytochrome c peroxidase. Chemical cleavage of the covalent complex has been used for a preliminary characterization of the site of cross-linking of cytochrome c to cytochrome c peroxidase. This linkage site was localized to the NH2 terminal part of cytochrome c peroxidase including residues 1-51.
D000596:Amino Acids / Q000032:analysis; D003488:Cyanogen Bromide; D003574:Cytochrome c Group / Q000031:analogs & derivatives* / Q000378:metabolism; D003578:Cytochrome-c Peroxidase / Q000378:metabolism*; D007700:Kinetics; D010446:Peptide Fragments / Q000032:analysis; D010544:Peroxidases / Q000378:metabolism*; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000596:Amino Acids; D003574:Cytochrome c Group; D010446:Peptide Fragments; D010544:Peroxidases; D003578:Cytochrome-c Peroxidase; D003488:Cyanogen Bromide