The Interaction of Arsenite with the Molybdenum Center of Chicken Liver Xanthine Dehydrogenase

✍ Scribed by Jean L. Johnson; K.V. Rajagopalan

• Book ID: 104106019
• Publisher: Elsevier Science
• Year: 1978
• Weight: 234 KB
• Volume: 8
• Category: Article
• ISSN: 0006-3061
• DOI: 10.1016/s0006-3061(00)80278-1

✦ Synopsis

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.