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Title: Binding of arylazidocytochrome c to yeast cytochrome c peroxidase. Author: Bisson R, Capaldi RA. Journal: J Biol Chem; 1981 May 10; 256(9):4362-7. PubMed ID: 6260796. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]