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Enhanced Ene‐Reductase Activity through Alteration of Artificial Nicotinamide Cofactor Substituents
Author(s) -
Löw Sebastian A.,
Löw Isabell M.,
Weissenborn Martin J.,
Hauer Bernhard
Publication year - 2016
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201501230
Subject(s) - cofactor , nicotinamide , chemistry , alkene , nad+ kinase , ene reaction , stereochemistry , stereocenter , biocatalysis , enzyme , hydride , combinatorial chemistry , reaction mechanism , organic chemistry , catalysis , metal , enantioselective synthesis
The reduction of activated C=C double bonds is an important reaction in synthetic chemistry owing to the potential formation of up to two new stereogenic centers. Artificial nicotinamide cofactors were recently presented as alternative suppliers of hydride equivalents needed for alkene reduction. To study the effect of cofactors on the reduction of activated alkenes, a set of N ‐substituted synthetic nicotinamide cofactors with differing oxidation potentials were synthesized and their electrochemical and kinetic behavior was studied. The effects of the synthetic cofactors on enzyme activity of four ene reductases are outlined in this study, where the cofactor mimic with an N ‐substituted 4‐hydroxy‐phenyl residue led to a sixfold higher v max relative to the natural cofactor NADH.