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

Journal Article · Sat Jan 31 23:00:00 EST 1981 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.78.2.664· OSTI ID:6507938

Scott, R A ^[1]; Cramer, S P; Shaw, R W; Beinert, H; Gray, H B

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1. Stanford Univ., CA

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/.

• OSTI ID: 6507938
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 78:2; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400301* -- Organic Chemistry-- Chemical & Physicochemical Properties-- (-1987)
BOND LENGTHS
CHEMICAL ANALYSIS
COPPER
CYTOCHROME OXIDASE
DIMENSIONS
ELEMENTS
ENZYMES
HAEM DEHYDROGENASES
LENGTH
METALS
NITROGEN
NONDESTRUCTIVE ANALYSIS
NONMETALS
OXIDOREDUCTASES
OXYGEN
SPECTRA
SULFUR
TRANSITION ELEMENTS
X-RAY EMISSION ANALYSIS
X-RAY FLUORESCENCE ANALYSIS
X-RAY SPECTRA