Preparation and characterization of the NAD vinylogue, 3-pyridylacryloamide adenine dinucleotide

Anderson, Bruce M.; Anderson, Christopher R.

doi:10.1016/0003-2697(91)90294-4

Cited by 2 publications

(1 citation statement)

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“…More conserved nicotinamide cofactor analogues, semisynthetic mNAD + s, were first prepared in the 1950s and 1960s by the group of Kaplan, this time used as the sole cofactor in oxidoreductase-catalyzed reactions to determine the mode of action of the cofactor and its steric and electronic properties within the enzymatic environment (vide infra). ,− Other types of 1,4-dihydropyridine derivatives, such as the Hantzsch ester 2,6-dimethyl-3,5-dicarboethoxy-1,4-dihydropyridine, are also used extensively as synthetic NAD(P)H analogues and for hydride transfer in catalytic metal-free reduction reactions. ,− The discussion on Hantzsch esters is beyond the scope of this review; however, it is relevant to mention that Hantzsch ester and its 1,4-dihydropyridine derivatives were discovered as effective calcium channel blockers and have wide applications in biomedical applications (see Section ) . Throughout the 1980s and 90s, Ohno and co-workers have published extensively on the use of NAD(P)H analogues in chemical synthesis for the reduction of a wide variety of compounds.…”

Section: State-of-the-art Of Synthetic Nicotinamide Cofactorsmentioning

confidence: 99%

Is Simpler Better? Synthetic Nicotinamide Cofactor Analogues for Redox Chemistry

2014

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The topic of synthetic nicotinamide cofactor analogues is resurfacing as new approaches are being explored, especially in the areas of organic chemistry and biocatalysis. By changing the adenine dinucleotide moiety for a simpler alkyl or aryl group and taking advantage of their ability for hydride transfer, these cofactor biomimetics are used in redox reactions in catalytic or stoichiometric amounts. Alteration of the amide functional group on the pyridine ring, thus varying their electronic properties, and the presence of divalent metal ions also enable rate acceleration in enzyme-catalyzed and chemical reactions. Herein, an overview of the synthesis, mechanism, and applications of nicotinamide cofactor NAD(P)H analogues in redox chemistry, particularly 1,4-dihydronicotinamide derivatives and their oxidized counterpart, is presented. These compounds have been extensively studied as models of NAD(P)H for enzymatic reactions with oxidoreductases as well as nonenzymatic reactions, and the focus of this review is placed mainly on the scope and limitations of these synthetic analogues in biocatalysis.

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