Equilibration of 1-Octanol with Alcohol Dehydrogenase. Evidence for Horse Liver Alcohol Dehydrogenase Responsibility for Exchange of the 1-pro-S Hydrogen Atom

Article abstract of DOI:10.1021/ja00344a037

Equilibration of hydrogen atoms of 1-octanol with water, mediated by the system horse liver alcohol dehydrogenase-NAD/NADH-diaphorase, involves a rapid exchange of 1-pro-R hydrogen atoms and a slow exchange of 1-pro-S hydrogen atoms.Yeast alcohol dehydrogenase has an apparent absolute stereospecificity for the 1-pro-R hydrogen atom of 1-octanol; replacement of horse liver dehydrogenase by yeast alcohol dehydrogenase in the above system results in exchange of only the 1-pro-R hydrogen atom of 1-octanol.In the absence of horse liver or yeast alcohol dehydrogenase, no exchange of C-1 hydrogen atoms of 1-octanol occurs.Thus, horse liver alcohol dehydrogenase is directly responsible for promoting exchange of the 1-pro-S hydrogen atom of 1-octanol with water hydrogen atoms.