Effects of vanadate on the molybdoproteins xanthine oxidase and nitrate reductase: kinetic evidence for multiple site interaction.
The inhibition of the activity of xanthine oxidase by vanadate was strikingly similar to vanadate inhibition of another molybdoprotein nitrate reductase. Although the main catalytic activity of both enzymes was inhibited, the partial NADH oxidase activity associated with these enzymes was stimulated several fold. It appears that the metal ion binds at multiple site in both enzymes. In the absence of any enzymes a combination of vanadium (V) and molybdenum (V) in air was found to oxide NADH rapidly.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002708:Chlorella / Q000201:enzymology; D004789:Enzyme Activation; D007700:Kinetics; D008892:Milk / Q000201:enzymology; D009565:Nitrate Reductases / Q000037:antagonists & inhibitors*; D011485:Protein Binding; D014639:Vanadium / Q000494:pharmacology*; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors*
D014639:Vanadium; D014969:Xanthine Oxidase; D009565:Nitrate Reductases