The nature of CuA in cytochrome c oxidase.

T. H. Stevens, C. T. Martin, H. Wang, G. W. Brudvig, C. P. Scholes, S. I. Chan

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Abstract

The isolation and purification of yeast cytochrome c oxidase is described. Characterization of the purified protein indicates that it is spectroscopically identical with cytochrome c oxidase isolated from beef heart. Preparations of isotopically substituted yeast cytochrome c oxidase are obtained incorporating [1,3-15N2]histidine or [beta,beta-2H2]cysteine. Electron paramagnetic resonance and electron nuclear double resonance spectra of the isotopically substituted proteins identify unambiguously at least 1 cysteine and 1 histidine as ligands to CuA and suggest that substantial spin density is delocalized onto a cysteine sulfur in the oxidized protein to render the site Cu(I)--S.

Original languageEnglish
Pages (from-to)12106-12113
Number of pages8
JournalJournal of Biological Chemistry
Volume257
Issue number20
Publication statusPublished - Oct 25 1982

ASJC Scopus subject areas

  • Biochemistry

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    Stevens, T. H., Martin, C. T., Wang, H., Brudvig, G. W., Scholes, C. P., & Chan, S. I. (1982). The nature of CuA in cytochrome c oxidase. Journal of Biological Chemistry, 257(20), 12106-12113.