title: Studies by electron paramagnetic resonance spectroscopy of xanthine oxidase enriched with molybdenum-95 and with molybdenum-97.
abstract: Investigations have been carried out on the nature of the species from the enzyme xanthine oxidase that give rise to two molybdenum (V) electron paramagnetic resonance (EPR) signals. Isotopic enrichment with 95Mo, 97Mo, 33S, and 17O was employed. Computer simulations of the EPR spectra recorded at 9- and 35-GHz microwave frequencies were used to evaluate the various hyperfine couplings and angular relations between the principal axes of g and A, as well as the nuclear electric quadrupole interaction for 97Mo. The results support the presence of an oxo ligand in the Rapid and of both an oxo and a sulfido ligand in the Very Rapid signal-giving species.
authors.affiliation: School of Chemistry and Molecular Sciences, University of Sussex, Brighton, U.K.
authors.forename: G N
authors.initials: GN
authors.lastname: George
authors.forename: R C
authors.initials: RC
authors.lastname: Bray
mesh_terms: D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D005260:Female; D007554:Isotopes; D008892:Milk / Q000201:enzymology; D008982:Molybdenum / Q000378:metabolism*; D011487:Protein Conformation; D014969:Xanthine Oxidase / Q000378:metabolism*
chemical_list: D007554:Isotopes; D008982:Molybdenum; D014969:Xanthine Oxidase