Abstract
This chapter discusses solvent isotope effects in the yeast alcohol dehydrogenase reaction in an effort to distinguish among possible modes of acid-base catalysis. Kinetic studies of the yeast alcohol dehydrogenase catalyzed interconversion of aromatic substrates indicate a rate limiting C-H bond cleavage step under steady state kinetic conditions, a distribution of charge at C-l of substrate in the transition state that is similar to that of alcohol, ρ+ = 0 for alcohol oxidation and a role for an active site residue, pK = 8.25, in acid-base catalysis. The simplest chemical mechanism, consistent with the observed data, has been proposed to involve concerted catalysis by a protonic base of hydride transfer. Solvent isotope effects were investigated in an effort to distinguish this mechanism from ones in which proton transfer is uncoupled from and fast relative to C-H bond cleavage.
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