Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase
- 1 November 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (23) , 5479-5488
- https://doi.org/10.1021/bi00318a016
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 8 references indexed in Scilit:
- Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 1. Liver alcohol dehydrogenase with benzyl alcohol and yeast aldehyde dehydrogenase with benzaldehydeBiochemistry, 1984
- Isotope effects on hydride transfer between NAD+ analogsJournal of the American Chemical Society, 1983
- Effect of isotope scrambling and tunneling on the kinetic and product isotope effects for reduced nicotinamide adenine dinucleotide model hydride transfer reactionsJournal of the American Chemical Society, 1983
- Mechanistic deductions from isotope effects in multireactant enzyme mechanismsBiochemistry, 1981
- Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenaseBiochemistry, 1981
- Kinetic and chemical mechanisms of yeast formate dehydrogenaseBiochemistry, 1980
- Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactionsBiochemistry, 1980
- Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesisAnalytical Biochemistry, 1979