title: Deuterium effects on binding of reduced coenzyme alcohol dehydrogenase isoenzyme EE.
abstract: Determination of dissociation constants by two different methods yield the following mean values in 20 millimolar phosphate, pH 7.0, 25 degrees C: 0.27 micromolar for reduced nicotinamide adenine dinucleotide (NADH); 0.29 micromolar for NADH with deuterium in the nicotinamide 4-B position (B-NADD); and 0.46 micromolar for NADH with deuterium in the nicotinamide 4-A position (A-NADD). These results indicate that dehydrogenases are capable of recognizing and distinguishing the appropriate hydrogen in the coenzyme already in the initial binding reaction.
mesh_terms: D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D003903:Deuterium; D005470:Fluorometry; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000032:analysis*; D009243:NAD / Q000032:analysis*
chemical_list: D007527:Isoenzymes; D009243:NAD; D003903:Deuterium; D007770:L-Lactate Dehydrogenase