Conformation of NAD+ bound to yeast and horse liver alcohol dehydrogenase in solution. The use of the proton-proton transferred nuclear Overhauser enhancement.

The glycosidic bond torsion angles and the conformations of the two riboses of NAD’ bound to yeast and horse liver alcohol dehydrogenase in solution have been determined by a novel method involving the measurement of proton-proton transferred nuclear Overhauser enhancements by ‘H-nuclear magnetic resonance. In both cases the conformation of the-a8eirosine and nicotinamide ribose is 3’-endo of the N type. The conformations about both glycosidic bonds are anti with xA (0-4’-C-l’-N-9-C-4) 270” and 240” for yeast and horse liver alcohol dehydrogenase, respectively, and xN (O-4’-C-l’-N-1-C-2) 240” for both yeast and horse liver alcohol dehydrogenase.