Communication—highly efficient electroenzymatic nadh regeneration by an electron-relay flavoenzyme

Sumi Lee; Hyunjun Choe; Dae Haeng Cho; Sung Ho Yoon; Keehoon Won; Yong Hwan Kima

doi:10.1149/2.0131606jes

Communication—highly efficient electroenzymatic nadh regeneration by an electron-relay flavoenzyme

Sumi Lee
, Hyunjun Choe
, Dae Haeng Cho
, Sung Ho Yoon
, Keehoon Won
, Yong Hwan Kima

Department of Chemical and Biochemical Engineering

Kwangwoon University
University of Florida
Kookmin University

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Efficient cofactor regeneration is essential for the utilization of many oxidoreductases. Herein, the β-subunit of formate dehydrogenase 1 from Methylobacterium extorquens AM1 (MeFDH1-β) was employed as a novel electroactive biocatalyst for electroenzymatic NADH regeneration for the first time. MeFDH1-β showed much better properties in both catalytic activity (a turnover frequency of 3,600 hr−¹) and current efficiency (ca. 98%) than a conventional rhodium (III)-based chemical catalyst (M = [Cp^∗Rh(bpy)H2O]²⁺, Cp^∗ = C₅Me₅, bpy = 2,2-bipyridine) and a traditional biocatalyst (diaphorase).

Original language	English
Pages (from-to)	G50-G52
Journal	Journal of the Electrochemical Society
Volume	163
Issue number	5
DOIs	https://doi.org/10.1149/2.0131606jes
State	Published - 2016

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 7 Affordable and Clean Energy

Access to Document

10.1149/2.0131606jes

Cite this

@article{aff89df94d714b9098246563afb9c5c4,

title = "Communication{\textemdash}highly efficient electroenzymatic nadh regeneration by an electron-relay flavoenzyme",

abstract = "Efficient cofactor regeneration is essential for the utilization of many oxidoreductases. Herein, the β-subunit of formate dehydrogenase 1 from Methylobacterium extorquens AM1 (MeFDH1-β) was employed as a novel electroactive biocatalyst for electroenzymatic NADH regeneration for the first time. MeFDH1-β showed much better properties in both catalytic activity (a turnover frequency of 3,600 hr−1) and current efficiency (ca. 98\%) than a conventional rhodium (III)-based chemical catalyst (M = [Cp∗Rh(bpy)H2O]2+, Cp∗ = C5Me5, bpy = 2,2-bipyridine) and a traditional biocatalyst (diaphorase).",

author = "Sumi Lee and Hyunjun Choe and Cho, \{Dae Haeng\} and Yoon, \{Sung Ho\} and Keehoon Won and Kima, \{Yong Hwan\}",

note = "Publisher Copyright: {\textcopyright} 2016 The Electrochemical Society.",

year = "2016",

doi = "10.1149/2.0131606jes",

language = "English",

volume = "163",

pages = "G50--G52",

journal = "Journal of the Electrochemical Society",

issn = "0013-4651",

publisher = "Institute of Physics",

number = "5",

}

TY - JOUR

T1 - Communication—highly efficient electroenzymatic nadh regeneration by an electron-relay flavoenzyme

AU - Lee, Sumi

AU - Choe, Hyunjun

AU - Cho, Dae Haeng

AU - Yoon, Sung Ho

AU - Won, Keehoon

AU - Kima, Yong Hwan

PY - 2016

Y1 - 2016

N2 - Efficient cofactor regeneration is essential for the utilization of many oxidoreductases. Herein, the β-subunit of formate dehydrogenase 1 from Methylobacterium extorquens AM1 (MeFDH1-β) was employed as a novel electroactive biocatalyst for electroenzymatic NADH regeneration for the first time. MeFDH1-β showed much better properties in both catalytic activity (a turnover frequency of 3,600 hr−1) and current efficiency (ca. 98%) than a conventional rhodium (III)-based chemical catalyst (M = [Cp∗Rh(bpy)H2O]2+, Cp∗ = C5Me5, bpy = 2,2-bipyridine) and a traditional biocatalyst (diaphorase).

AB - Efficient cofactor regeneration is essential for the utilization of many oxidoreductases. Herein, the β-subunit of formate dehydrogenase 1 from Methylobacterium extorquens AM1 (MeFDH1-β) was employed as a novel electroactive biocatalyst for electroenzymatic NADH regeneration for the first time. MeFDH1-β showed much better properties in both catalytic activity (a turnover frequency of 3,600 hr−1) and current efficiency (ca. 98%) than a conventional rhodium (III)-based chemical catalyst (M = [Cp∗Rh(bpy)H2O]2+, Cp∗ = C5Me5, bpy = 2,2-bipyridine) and a traditional biocatalyst (diaphorase).

UR - https://www.scopus.com/pages/publications/84963496443

U2 - 10.1149/2.0131606jes

DO - 10.1149/2.0131606jes

M3 - Article

AN - SCOPUS:84963496443

SN - 0013-4651

VL - 163

SP - G50-G52

JO - Journal of the Electrochemical Society

JF - Journal of the Electrochemical Society

IS - 5

ER -

Communication—highly efficient electroenzymatic nadh regeneration by an electron-relay flavoenzyme

Abstract

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this