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Product Distribution of Steady-State and Pulsed Electrochemical Regeneration of 1,4-NADH and Integration with Enzymatic Reaction.


ABSTRACT: The direct electrochemical reduction of nicotinamide adenine dinucleotide (NAD+) results in various products, complicating the regeneration of the crucial 1,4-NADH cofactor for enzymatic reactions. Previous research primarily focused on steady-state polarization to examine potential impacts on product selectivity. However, this study explores the influence of dynamic conditions on the selectivity of NAD+ reduction products by comparing two dynamic profiles with steady-state conditions. Our findings reveal that the main products, including 1,4-NADH, several dimers, and ADP-ribose, remained consistent across all conditions. A minor by-product, 1,6-NADH, was also identified. The product distribution varied depending on the experimental conditions (steady state vs. dynamic) and the concentration of NAD+, with higher concentrations and overpotentials promoting dimerization. The optimal yield of 1,4-NADH was achieved under steady-state conditions with low overpotential and NAD+ concentrations. While dynamic conditions enhanced the 1,4-NADH yield at shorter reaction times, they also resulted in a significant amount of unidentified products. Furthermore, this study assessed the potential of using pulsed electrochemical regeneration of 1,4-NADH with enoate reductase (XenB) for cyclohexenone reduction.

SUBMITTER: Al-Shaibani MAS 

PROVIDER: S-EPMC11319214 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature

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Product Distribution of Steady-State and Pulsed Electrochemical Regeneration of 1,4-NADH and Integration with Enzymatic Reaction.

Al-Shaibani Mohammed Ali Saif MAS   Sakoleva Thaleia T   Živković Luka A LA   Austin Harry P HP   Dörr Mark M   Hilfert Liane L   Haak Edgar E   Bornscheuer Uwe T UT   Vidaković-Koch Tanja T  

ChemistryOpen 20240412 8


The direct electrochemical reduction of nicotinamide adenine dinucleotide (NAD<sup>+</sup>) results in various products, complicating the regeneration of the crucial 1,4-NADH cofactor for enzymatic reactions. Previous research primarily focused on steady-state polarization to examine potential impacts on product selectivity. However, this study explores the influence of dynamic conditions on the selectivity of NAD<sup>+</sup> reduction products by comparing two dynamic profiles with steady-state  ...[more]

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