Deuterium effects on binding of reduced coenzyme alcohol dehydrogenase isoenzyme EE.
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.
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*
D007527:Isoenzymes; D009243:NAD; D003903:Deuterium; D007770:L-Lactate Dehydrogenase