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Molybdenum site of xanthine oxidase. Structural evidence from x-ray absorption spectroscopy

Journal Article · · J. Am. Chem. Soc.; (United States)
DOI:https://doi.org/10.1021/ja00504a069· OSTI ID:6063384
Xanthine oxidase was isolated from unpasteurized buttermilk by a standard procedure. Extended x-ray absorption fine structure (EXAFS) data indicate that reduced xanthine oxidase contains molybdenum in the four valence oxidation state. Curve fitting of the EXAFS data for oxidized xanthine oxidase suggests that there are two different Mo-ligand distances, 1.5 oxygen atoms at 1.71 A and 2 sulfur atoms at 2.54 A. Including a third sulfur atom at a longer distance significantly improved the fit. Several possible formulations are proposed. 2 figures, 1 table.
Research Organization:
Stanford Univ., CA
OSTI ID:
6063384
Journal Information:
J. Am. Chem. Soc.; (United States), Journal Name: J. Am. Chem. Soc.; (United States) Vol. 101:10; ISSN JACSA
Country of Publication:
United States
Language:
English