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• W4225253003 endingPage "140480" @default.
• W4225253003 startingPage "140480" @default.
• W4225253003 abstract "• NAD + /NADH-dependent FDH fused with solid-binding peptide retain biocatalytic activity. • Solid-binding of fusion enzymes depends on fusion site and tertiary structure. • Sbp fusion renders enzyme to electrode for facile interfacial electron transfer. • A platform for direct electrical contact of NAD + /NADH-dependent enzymes on the electrode surface is developed. • NADH oxidation and NAD + reduction at low overpotential for bioelectronics applications is established. NAD + /NADH-dependent redox enzymes constitute most known oxidoreductases, but their inherent complexity due to their reliance on the diffusional nature of soluble cofactors limits their application in bioelectrocatalytic systems. Herein, a gold-binding peptide (gbp) is genetically introduced at the NAD + /NADH-dependent formate dehydrogenase (FDH) to add a non-native gold-binding activity to directly wiring the enzyme to the electrode surface. Our gold-binding kinetics studies on the native and synthetic FDHs revealed that the gold-binding properties of the fused enzymes are highly dependent on the fusion site and that the tertiary structure of the fusion enzyme controls the efficiency of gold-binding domain display fusion. As such, the highest gold-binding activity was observed with the fusion of gbp at the C-terminus (FDH gbpC ), whereas binding at both termini FDH gbpNC and FDH gbpN appeared to be less active. Moreover, the presence of gbp increased the stability of an integrated enzyme electrode in the bioelectrocatalytic reactions occurring at the enzyme-electrode interface. Direct electrochemical NADH oxidation produced by the enzymatic reaction in the presence of formate and NAD + was observed at a low overpotential range of −0.45 to −0.15 V vs Ag/Ag + for all types of enzyme-electrodes, which indicates direct-electrical contact between the cofactor binding site and the electrode surface. The enhanced electron transfer kinetics could be explained by the shorter distance between the cofactor-binding site and electrode surface. Furthermore, the addition of NADH and CO 2 increased the reductive catalytic current, which suggested the enzymatic CO 2 reduction to formate using a hydride of NADH and a subsequent reduction of the generated NAD + . We demonstrated that biotechnology can directly contact enzymes onto the electrode surface, which has proven to be a reliable method for bio-electronic applications, especially involving NAD + /NADH-dependent enzymes." @default.
• W4225253003 created "2022-05-04" @default.
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• W4225253003 date "2022-07-01" @default.
• W4225253003 modified "2023-09-30" @default.
• W4225253003 title "Direct electrical contact of NAD+/NADH-dependent dehydrogenase on electrode surface enabled by non-native solid-binding peptide as a molecular binder" @default.
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• W4225253003 doi "https://doi.org/10.1016/j.electacta.2022.140480" @default.
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