The enthalpy change for the reduction of nicotinamide–adenine dinucleotide
- 1 November 1974
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 143 (2), 365-368
- https://doi.org/10.1042/bj1430365
Abstract
The heat of the reaction NAD++propan-2-ol=NADH+acetone+H+ was determined to be 42.5±0.6kJ/mol (10.17±0.15kcal/mol) from equilibrium measurements at 9–42°C catalysed by yeast alcohol dehydrogenase. With the aid of thermochemical data for acetone and propan-2-ol the values of ΔH=−29.2kJ/mol (−6.99kcal/mol) and ΔG0=22.1kJ/mol (5.28kcal/mol) are derived for the reduction of NAD (NAD++H2=NADH+H+). These values are consistent with analogous but less accurate data for the ethanol–acetaldehyde reaction. Thermodynamic data for the reduction of NAD and NADP are summarized.Keywords
This publication has 7 references indexed in Scilit:
- The equilibrium constants of the glutamate dehydrogenase systemsBiochemical Journal, 1967
- Kinetic studies of temperature changes and oxygen uptake in a differential calorimeter: The heat of oxidation of NADH and succinateArchives of Biochemistry and Biophysics, 1967
- The Effect of Temperature on the Oxidation-Reduction Potential of the Diphosphopyridine Nucleotide SystemJournal of Biological Chemistry, 1959
- On the temperature dependence and mechanism of action of alcohol dehydrogenaseBiochimica et Biophysica Acta, 1955
- The free-energy changes for the reduction of diphosphopyridine nucleotide and the dehydrogenation of l-malate and l-glycerol 1-phosphateBiochemical Journal, 1953
- The free-energy changes associated with the individual steps of the tricarboxylic acid cycle, glycolysis and alcoholic fermentation and with the hydrolysis of the pyrophosphate groups of adenosinetriphosphateBiochemical Journal, 1953
- CRYSTALLINE ALCOHOL DEHYDROGENASE FROM BAKERS' YEASTJournal of Biological Chemistry, 1950