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Liver alcohol dehydrogenase (LADH) enzyme reduces aldehydes to primary alcohols in the presence of NADH as a cofactor. We are measuring the catalytic activity of LADH under varying electronic environments by using substrates with electron donating and electron withdrawing groups located at the para position of the aldehyde. In order to determine the relative electronic environments of the substrates, Cyclic Voltammetry was used. The catalytic studies performed with substrates of various electronic environments allow for the determination of optimized polar effects for enzyme catalysis. In addition, we have used a synthetic cofactor N-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 overarching goal is to develop a set of optimized substrate and cofactor guidelines that will inform future studies with enzymes and their model systems.
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Sunderland, James Rainer, "Exploring the Kinetic Dependence on Electronic Environment of Substrates and Cofactors in Catalysis of Aromatic Aldehydes to Alcohols by Equine Liver Alcohol Dehydrogenase Enzyme" (2013). Senior Projects Spring 2013. 9.