title: A new irreversibly inhibited form of xanthine oxidase from ethylisonitrile.
abstract: The treatment of xanthine oxidase with ethylisonitrile results in irreversible inhibition of the catalytic activity. Chemical and spectroscopic evidence suggests that the inhibited enzyme is a new distinct derivative in which the essential sulfido ligand to molybdenum has been modified or removed.
authors.affiliation: Department of Chemistry, Wesleyan University, Middletown, CT 06459-0180, USA.
authors.forename: S A
authors.initials: SA
authors.lastname: Holmer
authors.forename: C L
authors.initials: CL
authors.lastname: Houlton
authors.forename: T D
authors.initials: TD
authors.lastname: Westmoreland
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy; D066298:In Vitro Techniques; D007700:Kinetics; D008024:Ligands; D015394:Molecular Structure; D008982:Molybdenum / Q000737:chemistry; D009570:Nitriles / Q000494:pharmacology*; D013440:Sulfides / Q000737:chemistry; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors*
chemical_list: D008024:Ligands; D009570:Nitriles; D013440:Sulfides; C001187:ethyl isocyanide; D008982:Molybdenum; D014969:Xanthine Oxidase