Investigation of liver alcohol dehydrogenase catalysis using an NADH biomimetic and comparison with a synthetic zinc model complex
作者: James R. SunderlandXingjian TaoElizabeth E. ButrickLauren C. KeilichChristine E. VillaJohn R. MiecznikowskiSwapan S. Jain
作者单位: 1Department of Chemistry, Bard College, 30 Campus Road, Annandale-on-Hudson, NY 12504, USA
2Department of Chemistry and Biochemistry, Fairfield University, 1073 North Benson Road, Fairfield, CT 06824, USA
刊名: Polyhedron, 2016, Vol.114 , pp.145-151
来源数据库: Elsevier Journal
DOI: 10.1016/j.poly.2015.11.027
关键词: BiomimeticSynthetic zinc model complexCatalysisCyclic voltammetryLiver alcohol dehydrogenase
英文摘要: Abstract(#br)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...
全文获取路径: Elsevier  (合作)
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影响因子:1.813 (2012)

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