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

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Electron Transport Complex IV
Cysteine
Electron Spin Resonance Spectroscopy
Histidine
Yeast
Yeasts
Beef
Proteins
Sulfur
Purification
Paramagnetic resonance
Ligands
Electrons

ASJC Scopus subject areas

  • Biochemistry

Cite this

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.

The nature of CuA in cytochrome c oxidase. / Stevens, T. H.; Martin, C. T.; Wang, H.; Brudvig, G. W.; Scholes, C. P.; Chan, S. I.

In: Journal of Biological Chemistry, Vol. 257, No. 20, 25.10.1982, p. 12106-12113.

Research output: Contribution to journalArticle

Stevens, TH, Martin, CT, Wang, H, Brudvig, GW, Scholes, CP & Chan, SI 1982, 'The nature of CuA in cytochrome c oxidase.', Journal of Biological Chemistry, vol. 257, no. 20, pp. 12106-12113.
Stevens TH, Martin CT, Wang H, Brudvig GW, Scholes CP, Chan SI. The nature of CuA in cytochrome c oxidase. Journal of Biological Chemistry. 1982 Oct 25;257(20):12106-12113.
Stevens, T. H. ; Martin, C. T. ; Wang, H. ; Brudvig, G. W. ; Scholes, C. P. ; Chan, S. I. / The nature of CuA in cytochrome c oxidase. In: Journal of Biological Chemistry. 1982 ; Vol. 257, No. 20. pp. 12106-12113.
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AU - Chan, S. I.

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AB - 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.

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