Theoretical study on CO2 reduction catalyzed by formate dehydrogenase using the cation radical of a bipyridinium salt with an ionic substituent as a co-enzyme

2020 ◽  
Vol 22 (46) ◽  
pp. 26987-26994
Author(s):  
Akimitsu Miyaji ◽  
Yutaka Amao
Keyword(s):  
Formate Dehydrogenase ◽  
Theoretical Study ◽  
Co2 Reduction ◽  
Cation Radical ◽  
Candida Boidinii ◽  
Theoretical Studies

Mechanism for formate dehydrogenase from Candida boidinii catalyzed CO2 reduction to formate with the cation radical of a 4,4′-bipyridinium salt with an ionic substituent as a co-enzyme was clarified by theoretical studies.

scholarly journals Visible-light-driven CO2 reduction to formate with a system of water-soluble zinc porphyrin and formate dehydrogenase in ionic liquid/aqueous media

RSC Advances ◽  
2020 ◽  
Vol 10 (69) ◽  
pp. 42354-42362
Author(s):  
Francesco Secundo ◽  
Yutaka Amao
Keyword(s):  
Ionic Liquid ◽  
Visible Light ◽  
Formate Dehydrogenase ◽  
Aqueous Media ◽  
Co2 Reduction ◽  
Water Soluble ◽  
Candida Boidinii ◽  
Zinc Porphyrin ◽  
Visible Light Driven ◽  
Soluble Zinc

Visible-light-driven CO2 reduction to formate with water-soluble zinc tetraphenylporphyrin tetrasulfonate, formate dehydrogenase from Candida boidinii and methylviologen in the presence of triethanolamine as an electron donor in an ionic liquid.

How does methylviologen cation radical supply two electrons to the formate dehydrogenase in the catalytic reduction process of CO2 to formate?

2020 ◽  
Vol 22 (33) ◽  
pp. 18595-18605 ◽  
Author(s):  
Akimitsu Miyaji ◽  
Yutaka Amao
Keyword(s):  
Quantum Chemical ◽  
Formate Dehydrogenase ◽  
Catalytic Reduction ◽  
Cation Radical ◽  
Reduction Process ◽  
Single Electron ◽  
Candida Boidinii ◽  
Chemical Analyses

The two-electron supply process using single-electron reduced methylviologen as a co-enzyme in the reduction process of CO2 to formate catalyzed by formate dehydrogenase from Candida boidinii was clarified by experimental and quantum chemical analyses.

Visible-light driven CO2 reduction to formate by the system of water-soluble zinc porphyrin and formate dehydrogenase with electron-mediated the amino and carbamoyl groups-modified viologen

2021 ◽  
Author(s):  
Akimitsu Miyaji ◽  
Yutaka Amao
Keyword(s):  
Visible Light ◽  
Formate Dehydrogenase ◽  
Co2 Reduction ◽  
Water Soluble ◽  
Candida Boidinii ◽  
Zinc Porphyrin ◽  
Visible Light Driven ◽  
Soluble Zinc

Visible-light driven CO2 reduction to formate with the system consisting of water-soluble zinc tetraphenylporphyrin tetrasulfonate (ZnTPPS), formate dehydrogenase from Candida boidinii (CbFDH) and 1-amino-1’-carbamoyl-4,4’- bipyridinium salt (ACBP) as an electron...

Artificial co-enzyme based on carbamoyl-modified viologen derivative cation radical for formate dehydrogenase in the catalytic CO2 reduction to formate

2020 ◽  
Vol 44 (43) ◽  
pp. 18803-18812
Author(s):  
Akimitsu Miyaji ◽  
Yutaka Amao
Keyword(s):  
Density Functional Theory ◽  
Kinetic Analysis ◽  
Density Functional ◽  
Formate Dehydrogenase ◽  
Density Functional Theory Calculation ◽  
Co2 Reduction ◽  
Cation Radical ◽  
Docking Simulation ◽  
Functional Theory ◽  
Theory Calculation

The interaction between the single-electron reduced carbamoyl-modified-4,4-bipyridinium salt and CbFDH in the CO2 reduction to formate is elucidated by enzymatic kinetic analysis, the docking simulation and density functional theory calculation.

Abnormal co-enzymatic behavior of a one-electron reduced bipyridinium salt with a carbamoyl group on the catalytic activity of CO2 reduction by formate dehydrogenase

2018 ◽  
Vol 42 (19) ◽  
pp. 15556-15560 ◽  
Author(s):  
S. Ikeyama ◽  
Y. Amao
Keyword(s):  
Catalytic Activity ◽  
Formate Dehydrogenase ◽  
Co2 Reduction ◽  
Candida Boidinii ◽  
Carbamoyl Group

A carbamoyl-modified bipyridinium salt has an enhancement and deactivation behaviour on the catalytic activity of CO2 reduction by formate dehydrogenase (FDH) from Candida boidinii.

Structural insights into the efficient CO2-reducing activity of an NAD-dependent formate dehydrogenase fromThiobacillussp. KNK65MA

2015 ◽  
Vol 71 (2) ◽  
pp. 313-323 ◽  
Author(s):  
Hyunjun Choe ◽  
Jung Min Ha ◽  
Jeong Chan Joo ◽  
Hyunook Kim ◽  
Hye-Jin Yoon ◽  
...  
Keyword(s):  
Formate Dehydrogenase ◽  
Computational Simulation ◽  
Candida Boidinii ◽  
Free Energy Barrier ◽  
Asymmetric Unit ◽  
Key Factors ◽  
Biological Unit ◽  
Practical Applications ◽  
Reducing Activity ◽  
Structural Insights

CO2fixation is thought to be one of the key factors in mitigating global warming. Of the various methods for removing CO2, the NAD-dependent formate dehydrogenase fromCandida boidinii(CbFDH) has been widely used in various biological CO2-reduction systems; however, practical applications of CbFDH have often been impeded owing to its low CO2-reducing activity. It has recently been demonstrated that the NAD-dependent formate dehydrogenase fromThiobacillussp. KNK65MA (TsFDH) has a higher CO2-reducing activity compared with CbFDH. The crystal structure of TsFDH revealed that the biological unit in the asymmetric unit has two conformations,i.e.open (NAD+-unbound) and closed (NAD+-bound) forms. Three major differences are observed in the crystal structures of TsFDH and CbFDH. Firstly, hole 2 in TsFDH is blocked by helix α20, whereas it is not blocked in CbFDH. Secondly, the sizes of holes 1 and 2 are larger in TsFDH than in CbFDH. Thirdly, Lys287 in TsFDH, which is crucial for the capture of formate and its subsequent delivery to the active site, is an alanine in CbFDH. A computational simulation suggested that the higher CO2-reducing activity of TsFDH is owing to its lower free-energy barrier to CO2reduction than in CbFDH.

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