Characterization of methylated azopyridine as a potential electron transfer mediator for electroenzymatic systems
![Thumbnail](/bitstream/handle/123456789/116689/Process%20Biochemistry.pdf.jpg?sequence=3&isAllowed=y)
View/ Open
Date
2017Author
Tetianec, Lidija
Baužienė, Ana
Kulys, Juozas
Jančienė, Regina
Marcinkevičienė, Liucija
Meškienė, Rita
Stankevičiūtė, Jonita
Meškys, Rolandas
Metadata
Show full item recordAbstract
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.