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Author Cramer, S. P. ♦ Shaw, R. W. ♦ Gray, H. B.
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY ♦ COPPER ♦ X-RAY SPECTRA ♦ CYTOCHROME OXIDASE ♦ BOND LENGTHS ♦ X-RAY FLUORESCENCE ANALYSIS ♦ NITROGEN ♦ SULFUR ♦ OXYGEN ♦ CHEMICAL ANALYSIS ♦ DIMENSIONS ♦ ELEMENTS ♦ ENZYMES ♦ HAEM DEHYDROGENASES ♦ LENGTH ♦ METALS ♦ NONDESTRUCTIVE ANALYSIS ♦ NONMETALS ♦ OXIDOREDUCTASES ♦ SPECTRA ♦ TRANSITION ELEMENTS ♦ X-RAY EMISSION ANALYSIS ♦ Organic Chemistry- Chemical & Physicochemical Properties- (-1987)
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 to 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 A and the average Cu-N (or Cu-O) distance is 1.97 +- 0.02 A. The amplitudes require ca. 1-1.5 sulfurs and 2 nitrogens (or oxygens) per copper. The distribution of sulfur ligands between Cu/sub A/ and Cu/sub B/ sites is not known, although there is some evidence that two sulfur atoms are bound to Cu/sub A/.
Educational Use Research
Learning Resource Type Article
Publisher Date 1981-02-01
Publisher Place United States
Volume Number 78
Issue Number 2


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