title: The interaction of arsenite with the molybdenum center of chicken liver xanthine dehydrogenase.
abstract: Inactivation of chicken liver xanthine dehydrogenase by arsenite is reflected in the molybdenum electron paramagnetic resonance signal at g = 1.97. The arsenite spectrum shows additional splittings and considerable broadening yet remains comparable to the native in total intensity. Further subtle alterations of the molybdenum signal of arsenite-treated enzyme are seen in the presence of purine-type substrates or inhibitors.
mesh_terms: D000818:Animals; D001151:Arsenic / Q000494:pharmacology; D002645:Chickens; D004578:Electron Spin Resonance Spectroscopy; D007658:Ketone Oxidoreductases / Q000037:antagonists & inhibitors; D008099:Liver / Q000201:enzymology*; D008982:Molybdenum; D011485:Protein Binding; D014968:Xanthine Dehydrogenase / Q000037:antagonists & inhibitors
chemical_list: D008982:Molybdenum; D014968:Xanthine Dehydrogenase; D007658:Ketone Oxidoreductases; D001151:Arsenic