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. 1981 Feb;78(2):664–667. doi: 10.1073/pnas.78.2.664

Extended x-ray absorption fine structure of copper in cytochrome c oxidase: Direct evidence for copper—sulfur ligation

Robert A Scott *, Stephen P Cramer †, Robert W Shaw ‡, Helmut Beinert ‡, Harry B Gray §
PMCID: PMC319859  PMID: 16592967

Abstract

The copper x-ray fluorescence excitation spectrum of cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) has been recorded in the 245—270 K range. The beat pattern observed in the extended x-ray absorption fine structure can be accounted for only by postulating a combination of sulfur and nitrogen (or oxygen) ligands to the copper. The average Cu—S distance is 2.27 ± 0.02 Å and the average Cu—N (or Cu—O) distance is 1.97 ± 0.02 Å. The amplitudes require ca, 1-1.5 sulfurs and 2 nitrogens (or oxygens) per copper. The distribution of sulfur ligands between CuA and CuB sites is not known, although there is some evidence that two sulfur atoms are bound to CuA.

Keywords: cytochrome aa3, copper sites, sulfur ligation, x-ray absorption spectroscopy, x-ray fluorescence detection

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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