Novel Artificial Coenzyme Based on Reduced Form of Diquat for Formate Dehydrogenase in the Catalytic Conversion of CO<sub>2</sub>to Formic Acid

Ikeyama, Shusaku; Abe, Ryutaro; Shiotani, Sachina; Amao, Yutaka

doi:10.1246/cl.160389

Cited by 16 publications

(9 citation statements)

References 28 publications

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“…The resultant k cat value of the reduced form of DC 2+ is the lowest compared with the other viologen derivatives. In this study, the effect of the functional group (amino or carboxyl group) in the reduced form of viologen derivatives on the CO 2 reduction activity with FDH was revealed and this result is important for the development of viologen derivatives for improvement of CO 2 reduction activity . We expect that controlling catalytic activity through manipulation of functional groups in artificial co‐enzymes will be applied in other enzyme systems.…”

Section: Resultsmentioning

confidence: 82%

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO₂ Reduction to Formic Acid with Formate Dehydrogenase

Ikeyama

Amao

2017

ChemCatChem

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Formate dehydrogenase (FDH) is an attractive catalyst for the reduction of CO2 because CO2 is converted to formic acid by FDH at room temperature under normal pressure in neutral aqueous solution. The reduced form of methylviologen acts as an artificial co‐enzyme for FDH in the conversion of CO2 to formic acid. To improve the catalytic activity of FDH in reducing CO2, viologen derivatives with ionic groups were synthesized as effective artificial co‐enzymes for FDH. We used enzyme kinetic analysis to assess the effect of the ionic amino or carboxyl functional groups in the reduced form of the viologen derivatives on the catalytic activity of FDH with respect to the reduction of CO2. By using 1,1′‐diaminoethyl‐4,4′‐bipyridinium salt, which is the reduced form of a viologen derivative with two amino groups, we optimized the reduction of CO2 to formic acid with FDH. The catalytic efficiency value (kcat/Km) of the reduced form of 1,1′‐diaminoethyl‐4,4′‐bipyridinium salt was estimated to be more than 560 times larger than that of the natural co‐enzyme NADH. From the analysis result, the CO2 reduction was influenced by the ionic group of the viologen derivative.

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Section: Resultsmentioning

confidence: 82%

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO₂ Reduction to Formic Acid with Formate Dehydrogenase

Ikeyama

Amao

2017

ChemCatChem

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“…In this system, the single‐electron reduced BPs act as a co‐enzyme for CbFDH instead of NADH. We previously reported the kinetic parameters of the single‐electron reduced various 4,4’‐ [27–30] and 2,2’‐BPs [31,32] for the CO 2 reduction to formate with CbFDH by using an enzymatic kinetic analysis. In order to elucidate the electron supply process using single‐electron reduced 4,4’‐BP as a co‐enzyme in the reduction process of CO 2 to formate catalyzed by CbFDH, moreover, the mechanism was clarified by experimental (enzyme reaction kinetics, electrochemical method) and quantum chemical analyses (docking simulation and density functional theory (DFT) calculation) [33] …”

Section: Introductionmentioning

confidence: 99%

Visible‐Light Driven CO₂ Reduction to Formate with Electron Mediated Nicotinamide‐Modified Viologen in the System of Water‐Soluble Zinc Porphyrin and Formate Dehydrogenase

Miyaji

Amao

2021

ChemNanoMat

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Visible‐light driven CO2 reduction to formate with the system consisting of water‐soluble zinc tetraphneylporphyrin tetrasulfonate (ZnTPPS), formate dehydrogenase from Candida boidinii (CbFDH) and 1‐nicotinamidethy‐1’‐methyl‐4,4’‐ bipyridinium salt (NEMBP) in the presence of triethanolamine (TEOA) as an electron donor was investigated. NEMBP was prepared as the 4,4’‐BP with the nicotinamide‐group to promote the improvement of affinity with CbFDH. The properties of NEMBP were characterized by photochemical and electrochemical methods. In order to evaluate the affinity between cation radical of NEMBP (NEMBP+.), as a co‐enzyme and CbFDH, the energy level based on simple docking simulation and density functional theory were estimated. It was speculated that NEMBP+. could bind near the substrate binding pocket of CbFDH as well as NAD+ by docking simulation. In the visible‐light driven NEMBP reduction with the sensitization of ZnTPPS in the presence of TEOA, the yield for reduction of NEMBP to NEMBP+. was estimated to be 80%. In the CO2 reduction to formate with the system consisting of TEOA, ZnTPPS, NEMBP and CbFDH, the turnover numbers of NEMBP and CbFDH were estimated to be 0.14 and 1.53 h−1, respectively.

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“…In addition, the biological stability of the modified cyanobacteria has yet to be improved for industrialization purposes [18][19][20][21][22]. Among the biological catalysts, Formate Dehydrogenase (FDH) enzymes are known to be reversible and several works have focused on the selective reduction reaction of CO2 into formate by extracted, purified and improved FDH [23,24]. Recently, the enzyme nitrogenase, a well-known N2-reducing enzyme, has also been reported to be able to catalyze the conversion of CO2 into formate and methane [25,26].…”

Section: Introductionmentioning

confidence: 99%

CO2 valorization by a new microbiological process

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Novel Artificial Coenzyme Based on Reduced Form of Diquat for Formate Dehydrogenase in the Catalytic Conversion of CO₂to Formic Acid

Cited by 16 publications

References 28 publications

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO₂ Reduction to Formic Acid with Formate Dehydrogenase

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO₂ Reduction to Formic Acid with Formate Dehydrogenase

Visible‐Light Driven CO₂ Reduction to Formate with Electron Mediated Nicotinamide‐Modified Viologen in the System of Water‐Soluble Zinc Porphyrin and Formate Dehydrogenase

CO2 valorization by a new microbiological process

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Novel Artificial Coenzyme Based on Reduced Form of Diquat for Formate Dehydrogenase in the Catalytic Conversion of CO2to Formic Acid

Cited by 16 publications

References 28 publications

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO2 Reduction to Formic Acid with Formate Dehydrogenase

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO2 Reduction to Formic Acid with Formate Dehydrogenase

Visible‐Light Driven CO2 Reduction to Formate with Electron Mediated Nicotinamide‐Modified Viologen in the System of Water‐Soluble Zinc Porphyrin and Formate Dehydrogenase

CO2 valorization by a new microbiological process

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Novel Artificial Coenzyme Based on Reduced Form of Diquat for Formate Dehydrogenase in the Catalytic Conversion of CO₂to Formic Acid

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO₂ Reduction to Formic Acid with Formate Dehydrogenase

An Artificial Co‐enzyme Based on the Viologen Skeleton for Highly Efficient CO₂ Reduction to Formic Acid with Formate Dehydrogenase

Visible‐Light Driven CO₂ Reduction to Formate with Electron Mediated Nicotinamide‐Modified Viologen in the System of Water‐Soluble Zinc Porphyrin and Formate Dehydrogenase