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Binding of cytochrome c to cytochrome c - oxidase in intact mitochondria. A study with radioactive photoaffinity-labeled cytochrome c

descriptionPublicationkeyboard_double_arrow_right Article 01 Feb 1980 English Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 92, pages 743-748 (issn: 0006-291X,

Authors: David F. Wilson; Reiko Oshino; Maria Erecińska;

doi: 10.1016/0006-291x(80)90766-4

pmid: 6244817

Binding of cytochrome c to cytochrome c - oxidase in intact mitochondria. A study with radioactive photoaffinity-labeled cytochrome c

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Abstract

Abstract [3H]-p-Azidophenacylbromide-(methyl-4-mercaptobutyrimidate)-cytochrome c from Saccharomyces cerevisiae was prepared and its properties determined. The radioactive photoaffinity-labeled cytochrome c was linked by irradiation into a covalent complex with cytochrome c oxidase. Analysis of the complex on SDS-polyacrylamide gels showed that cytochrome c bound to one of the smaller subunits of cytochrome c oxidase with an apparent molecular weight of 15,000.

Related Organizations

University of Pennsylvania
United States

Keywords

Electron Transport Complex IV, Molecular Weight, Macromolecular Substances, Affinity Labels, Cytochrome c Group, Saccharomyces cerevisiae, Tritium, Mitochondria, Protein Binding

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