Oxidoreduction between Cycloalkanols and Cycloalkanones in the Cultured Cells of Nicotiana tabacum. Correlation of the Reaction Rate with the 13C NMR Chemical Shift of the Carbonyl Carbon
- 5 December 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Chemistry Letters
- Vol. 15 (12) , 2053-2056
- https://doi.org/10.1246/cl.1986.2053
Abstract
The enzyme system responsible for the oxidoreduction between cycloalkanols and their corresponding cycloalkanones in the cultured cells of Nicotiana tabacum was found to be alcohol dehydrogenase which is similar to the dehydrogenase from tea seeds and horse liver. The rate constants and the equilibrium constants of the oxidoreduction between the cycloalkanols and their corresponding cycloalkanones with this enzyme system were well correlated with the 13C NMR chemical shift of the carbonyl carbon of the oxidation products, i.e., the cycloalkanones.Keywords
This publication has 6 references indexed in Scilit:
- Oxidation-reduction relationship between cycloalkanones and the corresponding cycloalkanols in a cell suspension culture of Nicotiana tabacumPlant Cell Reports, 1983
- Enzymes in organic syntheses. 19. Evaluation of the stereoselectivities of horse liver alcohol dehydrogenase; catalyzed oxidoreductions of hydroxy- and ketothiolanes, -thianes, and -thiepanesCanadian Journal of Chemistry, 1981
- Self-Consistent Molecular Orbital Methods. XI. Molecular Orbital Theory of NMR Chemical ShiftsThe Journal of Chemical Physics, 1971
- Substrate inhibition effects in the liver alcohol dehydrogenase reactionArchives of Biochemistry and Biophysics, 1966
- Chemical effects of steric strains—XIVTetrahedron, 1957
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934