Reference: Bisson R and Capaldi RA (1981) Binding of arylazidocytochrome c to yeast cytochrome c peroxidase. J Biol Chem 256(9):4362-7

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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.

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Journal Article | Research Support, U.S. Gov't, P.H.S.
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Bisson R, Capaldi RA
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