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.

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.

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...

scholarly journals Effect of confinement of horse heart cytochrome c and formate dehydrogenase from Candida boidinii on mesoporous carbons on their catalytic activity

2021 ◽  
Author(s):  
Naiara Hernández-Ibáñez ◽  
Vicente Montiel ◽  
Alicia Gomis-Berenguer ◽  
Conchi Ania ◽  
Jesús Iniesta
Keyword(s):  
Catalytic Activity ◽  
Cytochrome C ◽  
Formic Acid ◽  
Formate Dehydrogenase ◽  
Direct Electron Transfer ◽  
Candida Boidinii ◽  
Mesoporous Carbons ◽  
Horse Heart Cytochrome ◽  
Pore Sizes ◽  
Cyt C

AbstractThis study reports the immobilization of two biocatalysts (e.g., cytochrome c—Cyt c—and the non-metalloenzyme formate dehydrogenase from Candida boidinii–cbFDH) on a series of mesoporous carbons with controlled pore sizes. The catalytic activity of the nanoconfined proteins was correlated with the pore size distribution of the carbon materials used as supports. The electrochemical behaviour of nanoconfined Cyt c showed direct electron transfer electroactivity in pore sizes matching tightly the protein dimension. The pseudo-peroxidase activity towards H2O2 reduction was enhanced at pH 4.0, due to the protein conformational changes. For cbFDH, the reduction of CO2 towards formic acid was evaluated for the nanoconfined protein, in the presence of nicotinamide adenine dinucleotide (NADH). The carbons displayed different cbFDH uptake capacity, governed by the dimensions of the main mesopore cavities and their accessibility through narrow pore necks. The catalytic activity of nanoconfined cbFDH was largely improved, compared to its performance in free solution. Regardless of the carbon support used, the production of formic acid was higher upon immobilization with lower nominal cbFDH:NADH ratios.

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.

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