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Characterization of Biomimetic Cofactors According to Stability, Redox Potentials, and Enzymatic Conversion by NADH Oxidase from Lactobacillus pentosus
Author(s) -
Nowak Claudia,
Pick André,
Csepei LénárdIstván,
Sieber Volker
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700258
Subject(s) - cofactor , nicotinamide , chemistry , enzyme , redox , oxidase test , combinatorial chemistry , biochemistry , organic chemistry
Oxidoreductases are attractive biocatalysts that convert achiral substrates into products of higher value, but they are also for the most part dependent on nicotinamide cofactors. Recently, biomimetic nicotinamide derivatives have received attention as less costly alternatives to natural cofactors. However, recycling of biomimetics is still challenging because there are only limited opportunities. Here, we have characterized various biomimetic cofactors with regard to stability and redox potentials to find the best alternative to natural cofactors. Further, the cofactor spectrum of NADH oxidase from Lactobacillus pentosus ( Lp Nox) could be expanded, and the enzymatic activity was also compared to activities with different small‐molecule catalysts. As a result, we succeeded in identifying several strategies for regeneration of oxidized biomimetics.