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We have compared the catalytic activity of horse liver alcohol dehydrogenase (LADH) with a synthetic zinc model complex in the presence of N-benzyl-1,4-dihydronicotinamide (BNAH), a cofactor which serves as a biomimetic for the natural cofactor NADH. We have used five different substrates (benzaldehyde, p-anisaldehyde, 4-nitrobenzaldehyde, 2-pyridine carboxaldehyde, and 5-pyrimidine carboxaldehyde) in this study. These substrates vary in their substituent inductive effect, which is the ability to donate or withdraw electron density away from their carbonyl-functional group. Our results reveal that in the presence of NADH, geometric factors (induced fit of the substrate and cofactor in the enzyme active site) are vital. However, reactivity assays show that in the presence of BNAH, there is a strong correlation between substrate electronic environment and the observed catalytic rate, i.e. the more electron withdrawn the substrate, the greater the speed at which the reduction reaction occurs. NMR spectroscopy reveals that a synthetic zinc model complex catalyzes the reduction of substrates in a manner consistent with LADH enzyme.


Copyright 2016 Elsevier

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Sunderland, J. R., Tao, X., Butrick, E. E., Keilich, L. C., Villa, C. E., Miecznikowski, J. R., & Jain, S. S. (2016). Investigation of liver alcohol dehydrogenase catalysis using an NADH biomimetic and comparison with a synthetic zinc model complex. Polyhedron, 114, 145-151.



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