Hydrogen exchange at the amide group of reduced pyridine nucleotides and the inhibition of that reaction by dehydrogenases.
Stopped flow ultraviolet spectroscopy has been used to measure the rate of hydrogen exchange with solvent at the amide group of reduced nicotinamide nucleotide coenzymes. Several mechanisms for the exchange reaction are considered in the light of the kinetic data. Complex formation between the coenzyme and any of four dehydrogenases markedly slows the rate of hydrogen exchange. Hydrogen bond formation and/or hydrophobic interactions within these complexes are thought to be the reasons for the decreased rate of exchange.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D009243:NAD; D009249:NADP; D009537:Nicotinamide Mononucleotide; D010084:Oxidation-Reduction; D011485:Protein Binding; D012265:Ribonucleotides; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013056:Spectrophotometry, Ultraviolet
D012265:Ribonucleotides; D009243:NAD; D009537:Nicotinamide Mononucleotide; D009249:NADP; D000429:Alcohol Oxidoreductases; D007770:L-Lactate Dehydrogenase; D005969:Glutamate Dehydrogenase