Direct reduction of NAD+ by electrochemical procedure and application of the regenerated NADH to enzyme reaction

Yun, Se-Eok; Taya, Masahito; Tone, Setsuji

doi:10.1007/bf01022402

Cited by 12 publications

(6 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Prior studies of NADH regeneration at metallic Pt electrodes—as opposed to the Pt/Al 2 O 3 system coupled with alcohol dehydrogenase, which exhibited 100% selective generation of 1,4‐NADH at low TOF—only partially characterized the products obtained. Yun et al . reported that enzymatically active NADH was produced with a selectivity of 65–70%.…”

Section: Resultsmentioning

confidence: 99%

Photoelectrochemical NADH Regeneration using Pt‐Modified p‐GaAs Semiconductor Electrodes

2017

View full text Add to dashboard Cite

Cofactor regeneration in enzymatic reductions is crucial for the application of enzymes to both biological and energy-related catalysis. Specifically, regenerating NADH from NAD + is of great interest, and using electrochemistry to achieve this end is considered a promising option. Here, we report the first example of photoelectrochemical NADH regeneration at the illuminated (l > 600 nm), metal-modified, p-type semiconductor electrode Pt/p-GaAs. Although bare p-GaAs electrodes produce only enzymatically inactive NAD 2 , NADH was produced at the illuminated Pt-modified p-GaAs surface. At low overpotential (À0.75 V vs. Ag/AgCl), Pt/p-GaAs exhibited a seven-fold greater faradaic efficiency for the formation of NADH than Pt alone, with reduced competition from the hydrogen evolution reaction. Improved faradaic efficiency and low overpotential suggest the possible utility of Pt/p-GaAs in energy-related NADHdependent enzymatic processes. Scheme 1. Structure of NAD + (nicotinamide) and two-electron redox conversion between NAD + and NADH (1,4-dihydronicotinamide), which occurs in enzymatic processes (ADPR = adenosine diphosphoribose).

show abstract

Section: Resultsmentioning

confidence: 99%

Photoelectrochemical NADH Regeneration using Pt‐Modified p‐GaAs Semiconductor Electrodes

2017

View full text Add to dashboard Cite

show abstract

“…At the moment, the authors of this paper do not have any explicit explanation that could be used to justify the low yield of 1,4-NADH obtained at −1.30 and −1.40 V. However, based on the findings reported in Jaegfeldt's paper [41] we could also assume that the significant increase in pH (above 11) recorded during the electrolysis of NAD + on RuGC at −1.30 and −1.40 V facilitates the formation of inactive 1,6-NADH instead of active 1,4-NADH, which is opposite to the situation recorded at lower overpotentials. Yun et al [40] have also reported that the amount of enzymatically active 1,4-NADH regenerated using a platinum electrode and a cell modified with an anion-charge membrane depends on the electrolysis overpotential applied. They have related the lower yield of 1,4-NADH obtained at higher overpotentials to the formation of the dimer.…”

Section: Batch Electrolysis-regeneration Of Nadhmentioning

confidence: 97%

“…50% at higher regeneration overpotentials up to ca. 65% at lower regeneration overpotentials [40]. Table 2 shows the yield (in percent) of enzymatically active 1,4-NADH formed at various electrolysis potentials.…”

Section: Batch Electrolysis-regeneration Of Nadhmentioning

confidence: 99%

Direct regeneration of NADH on a ruthenium modified glassy carbon electrode

Azem

Man

Omanovic

2004

Journal of Molecular Catalysis A: Chemical

View full text Add to dashboard Cite

“…The electrochemical regeneration of NAD(P)H has to be performed by indirect electrochemical methods, as direct reduction requires high overpotentials and results in production of inactive dinucleotide-dimers (12,13). One approach to overcome dimer formation used a silver electrode at −480 mV vs. NHE covered by an anion-exchange membrane (14). Only three total turnovers for NAD to NADH conversion were reported.…”

Section: Nad(p)h Regenerationmentioning

confidence: 99%

Challenges in capturing oxygenase activity in vitro

Vilker

Reipa

Mayhew

et al. 1999

J Americ Oil Chem Soc

View full text Add to dashboard Cite

Biocatalysis using oxygenase or desaturase enzymes has the potential to add value to native fats and oils by adding oxygen, hydroxyl groups, or double bonds to create regio-and/or stereospecific products. These enzymes are a subset of the large class of oxidoreductase enzymes (from EC subgroups 1.13 and 1.14) involved with biological oxidation and reduction. In vitro biocatalytic processing using these enzymes is hampered by the high cost of the stoichiometric cofactors. This article reviews recent progress in developing in vitro redox enzyme biocatalysis for commercial-scale syntheses. Coenzyme recycling and electrochemical redox cycling as methods for cofactor regeneration are described and commercial applications indicated. Direct charge transfer without use of mediators is described as the cleanest way of introducing the reducing power into the catalytic cycle. Our electrochemically driven cytochrome P450 cam bioreactor is discussed as an example of direct charge transfer to a redox protein. Site-directed mutagenesis in the active site of the P450 cam monooxygenase greatly improved performance for the conversion of the nonnative substrate, styrene to styrene oxide. This epoxidation reaction was also shown to give a single product (styrene oxide) in the bioelectrochemical reactor when the diatomic oxygen co-substrate was managed properly.

show abstract

Direct reduction of NAD+ by electrochemical procedure and application of the regenerated NADH to enzyme reaction

Cited by 12 publications

References 12 publications

Photoelectrochemical NADH Regeneration using Pt‐Modified p‐GaAs Semiconductor Electrodes

Photoelectrochemical NADH Regeneration using Pt‐Modified p‐GaAs Semiconductor Electrodes

Direct regeneration of NADH on a ruthenium modified glassy carbon electrode

Challenges in capturing oxygenase activity in vitro

Contact Info

Product

Resources

About