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NAD + Cofactor Regeneration by TMB‐Mediated Horseradish‐Peroxidase‐Catalyzed Reactions
Author(s) -
Li Yunzhe,
Wang ZhenGang,
Li Huanrong,
Ding Baoquan
Publication year - 2018
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201801731
Subject(s) - nad+ kinase , horseradish peroxidase , cofactor , nicotinamide adenine dinucleotide , chemistry , peroxidase , substrate (aquarium) , catalysis , enzyme , dehydrogenase , nicotinamide , enzyme catalysis , biochemistry , stereochemistry , biology , ecology
The regeneration of nicotinamide adenine dinucleotide (NAD + ) has attracted substantial interest in the enzymatic chemical transformations. In this work, we report the use of a traditional horseradish peroxidase (HRP)/H 2 O 2 system for the catalytic transformation of reduced nicotinamide adenine dinucleotide (NADH) into NAD + , in the presence of a common HRP substrate, 3,3′,5,5′‐tetramethylbenzidine (TMB), as an electron mediator. The effect of H 2 O 2 , HRP or TMB concentration on the oxidization rate of NADH was systematically investigated. The results show that a small amount of HRP and TMB resulted in high efficient oxidization of NADH into NAD + , through the switching between the oxidized and reduced states of TMB. The enzymatic system also exhibited pH‐dependent catalytic properties, so that a XOR logic gate was constructed with H 2 O 2 and H + as the gate inputs, and the generated TMB charge transfer complex as the output signals. The addition of glucose dehydrogenase (GDH)/glucose allows the cycling between the NADH and NAD + and the coupled activation of HRP and GDH. This work provides a strategy for efficient regeneration of the NAD + cofactor and enzyme‐driven transformations.