Liver alcohol dehydrogenase (LADH) enzyme reduces aldehydes to primary alcohols in the presence of NADH as a cofactor. We are measuring the catalytic efficiency of LADH under varying electronic environments by using substrates with electron donating and electron withdrawing groups located at the para position of the aldehyde. These studies allow for the determination of optimized polar effects for enzyme catalysis. In addition, we have used a synthetic cofactor 1-benzyl-1,4-dihydronicotinamide (BNAH) as opposed to the natural biological cofactor, nicotinamide adenine dinucleotide (NADH). While there are structural differences between the two molecules, both can operate as cofactors in the reactions catalyzed by LADH. This work is therefore also an analysis of enzymatic efficiency in the presence of cofactor analogs. Our work complements studies where synthetic pincer complexes have been used as model LADH active sites. Our overarching goal is to develop a set of optimized substrate and cofactor guidelines that will inform future studies with enzymes and their model systems.

Investigating the effect of substrate electronic environment on liver alcohol dehydrogenase catalysis

244th National Meeting (2012)

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