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- W2033486561 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 Cu A and Cu B sites is not known, although there is some evidence that two sulfur atoms are bound to Cu A ." @default.
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- W2033486561 date "1981-02-01" @default.
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- W2033486561 title "Extended x-ray absorption fine structure of copper in cytochrome <i>c</i> oxidase: Direct evidence for copper—sulfur ligation" @default.
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- W2033486561 doi "https://doi.org/10.1073/pnas.78.2.664" @default.
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