Binding of Au(CN)2- and Pt(CN)4-2- to horse liver alcohol dehydrogenase. A 35C1NMR relaxation study.
The binding of Au(CN)2- and Pt(CN)4-2- ions to the coenzyme binding site of horse liver alcohol dehydrogenase (alcohol : NAD+ oxidoreductase EC 1.1.1.1) has been studied by 35C1 nuclear magnetic relaxation. Longitudinal relaxation rates were analyzed in terms of a simple model and binding constants for Au(CN)2-, Pt(CN)4-2- and C1- were estimated. From a comparison between transverse and longitudinal relaxation rates the correlation time and the quadrupole coupling constant of bound chloride ion were obtained. The quadrupole coupling constant estimated from a simple electrostatic model for chloride ion interacting with an arginine group agrees with the experimental value.
D000429:Alcohol Oxidoreductases; D000818:Animals; D001120:Arginine; D001665:Binding Sites; D002713:Chlorine; D003486:Cyanides; D006046:Gold; D006736:Horses; D008099:Liver / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009243:NAD / Q000494:pharmacology; D010984:Platinum; D011485:Protein Binding; D011868:Radioisotopes
D003486:Cyanides; D011868:Radioisotopes; D009243:NAD; D010984:Platinum; D002713:Chlorine; D006046:Gold; D001120:Arginine; D000429:Alcohol Oxidoreductases