Characterization of methylated azopyridine as a potential electron transfer mediator for electroenzymatic systems |
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| Affiliation: | 1. Institute of Biochemistry, Life Science Center, Vilnius University, Sauletekio al. 7, LT-10257, Vilnius, Lithuania;2. Department of Chemistry and Bioengineering, Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Sauletekio al. 11, LT-10223, Vilnius, Lithuania;1. Department of Medicine, University of Illinois at Chicago, Chicago, IL, United States;2. Jesse Brown VA Medical Center, Chicago, IL, United States;3. Department of Urology, University of Illinois at Chicago, Chicago, IL, United States;1. Key Laboratory of Artificial Micro- and Nano-Structures of Ministry of Education, School of Physics and Technology, Wuhan University, Wuhan 430072, PR China;2. Laboratory of Printable Functional Nanomaterials and Printed Electronics, School of Printing and Packaging, Wuhan University, Wuhan 430072, PR China;1. Institute of Biosciences, TU Bergakademie Freiberg, Leipziger Str. 29, Freiberg 09599, Germany;2. Department of Chemical Engineering, Silesian University of Technology, M. Strzody 7, Gliwice 44-100, Poland |
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| Abstract: | N,N'-dimethyl-4,4'-azopyridinium methyl sulfate (MAZP) was characterized as an electron transfer mediator for oxidation reactions catalyzed by NAD+- and pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenases. The bimolecular rate constant of NADH reactivity with MAZP was defined as (2.2 ± 0.1) × 105 M−1 s−1, whereas the bimolecular rate constant of reactivity of the reduced form of PQQ-dependent alcohol dehydrogenase with MAZP was determined to be (4.7 ± 0.1) × 104 M−1 s−1. The use of MAZP for the regeneration of the cofactors was investigated by applying the electrochemical oxidation of the mediator. The total turnover numbers of mediator MAZP and cofactor NADH for ethanol oxidation catalyzed by NAD+-dependent alcohol dehydrogenase depended on the concentration of the substrate and the duration of the electrolysis, and the yield of the reaction was limited by the enzyme inactivation and the electrochemical process. The PQQ-dependent alcohol dehydrogenase was more stable, and the turnover number of the enzyme reached a value of 2.3 × 103. In addition, oxidation of 1,2-propanediol catalyzed by the PQQ-dependent alcohol dehydrogenase proceeded enantioselectively to yield l-lactic acid. |
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| Keywords: | Methylated azopyridine Quinoprotein Alcohol dehydrogenase NADH Cofactor regeneration Enantioselective conversion |
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