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Extended X-ray absorption fine structure of copper in Cu/sub A/-depleted, p-(hydroxymercuri)benzoate-modified, and native cytochrome c oxidase

Journal Article · · Biochemistry; (United States)
OSTI ID:5511446
Cytochrome c oxidase contains four redox-active metal centers: two heme irons, cytochromes a and a/sub 3/, and two copper ions, Cu/sub A/ and Cu/sub B/. Due to the paucity of spectroscopic signatures for both copper sites in cytochrome c oxidase, the ligands and structures for these sites have remained ambiguous. The specific depletion of Cu/sub A/ from the p-(hydroxymercuri)benzoate- (pHMB-) modified cytochrome c oxidase recently reported is herein described. Characterization of this enzyme shows that the structures of the remaining metal centers are essentially unperturbed by the Cu/sub A/ modification and depletion. Copper extended X-ray absorption fine structure (EXAFS) measurements on the Cu/sub A/-depleted cytochrome c oxidase reveal coordination of three (N, O) ligands and one (S, Cl) ligand at the Cu/sub B/ site. Comparison of EXAFS results obtained for the Cu/sub A/-depleted, pHMB-modified, and unmodified control enzymes has allowed the deconvolution of the EXAFS in terms of the inner coordination spheres for Cu/sub A/ as well as Cu/sub B/. On the basis of these data, it is found that the structure for the Cu/sub A/ site is consistent with two (N,O) ligands and two S ligands.
Research Organization:
California Institute of Technology, Pasadena
OSTI ID:
5511446
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:8; ISSN BICHA
Country of Publication:
United States
Language:
English