A new irreversibly inhibited form of xanthine oxidase from ethylisonitrile.
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.
Holmer
S A
SA
Department of Chemistry, Wesleyan University, Middletown, CT 06459-0180, USA.
Houlton
C L
CL
Westmoreland
T D
TD
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*
D008024:Ligands; D009570:Nitriles; D013440:Sulfides; C001187:ethyl isocyanide; D008982:Molybdenum; D014969:Xanthine Oxidase