Reports

Deuterium Effects on Binding of Reduced Coenzyme Alcohol Dehydrogenase Isoenzyme EE

Science  30 Apr 1971:
Vol. 172, Issue 3982, pp. 478-480
DOI: 10.1126/science.172.3982.478

Abstract

Determination of dissociation constants by two different methods yield the following mean values in 20 millimolar phosphate, pH 7.0, 25°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.

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