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Stevens TH, et al.  (1982) The nature of CuA in cytochrome c oxidase. J Biol Chem 257(20):12106-13

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.FAU - Stevens, T .

Status: Published Type: Journal Article | Research Support, U.S. Gov't, P.H.S. PubMed ID: 6288707

Topics addressed in this paper

Number of different genes curated to this paper: 21

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Topics Genes linked to topics (#1 - 10 )
COX1 COX10 COX11 COX12 COX13 COX14 COX15 COX16 COX17 COX18
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Protein Physical Properties blue ball blue ball blue ball blue ball blue ball blue ball blue ball blue ball blue ball blue ball
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Topics Genes linked to topics (#11 - 20 )
COX19 COX2 COX20 COX3 COX4 COX5A COX5B COX6 COX7 COX8
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Topics Genes linked to topics (#21 )
COX9
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