Production and separation of formate dehydrogenase from Candida boidinii

2007 ◽  
Vol 40 (4) ◽  
pp. 940-946 ◽  
Author(s):  
Yunling Bai ◽  
Shang-Tian Yang
Keyword(s):  
Formate Dehydrogenase ◽  
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.

scholarly journals Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions

2019 ◽  
Vol 74 (3-4) ◽  
pp. 101-104 ◽  
Author(s):  
Milja Pesic ◽  
Sébastien Jean-Paul Willot ◽  
Elena Fernández-Fueyo ◽  
Florian Tieves ◽  
Miguel Alcalde ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Formate Dehydrogenase ◽  
Flavin Mononucleotide ◽  
Candida Boidinii ◽  
Reaction Parameters ◽  
Old Yellow Enzyme ◽  
Hydroxylation Reaction ◽  
In Situ Generation ◽  
Hydrogen Peroxide Generation

Abstract There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in a stereoselective fashion and with high catalytic efficiencies, while using hydrogen peroxide or organic peroxides as oxidant. However, enzymes belonging to this class exhibit a very low stability in the presence of peroxides. With the aim of bypassing this fast and irreversible inactivation, we study the use of a gradual supply of hydrogen peroxide to maintain its concentration at stoichiometric levels. In this contribution, we report a multienzymatic cascade for in situ generation of hydrogen peroxide. In the first step, in the presence of NAD+ cofactor, formate dehydrogenase from Candida boidinii (FDH) catalysed the oxidation of formate yielding CO2. Reduced NADH was reoxidised by the reduction of the flavin mononucleotide cofactor bound to an old yellow enzyme homologue from Bacillus subtilis (YqjM), which subsequently reacts with molecular oxygen yielding hydrogen peroxide. Finally, this system was coupled to the hydroxylation of ethylbenzene reaction catalysed by an evolved peroxygenase from Agrocybe aegerita (rAaeUPO). Additionally, we studied the influence of different reaction parameters on the performance of the cascade with the aim of improving the turnover of the hydroxylation reaction.

Carbonic anhydrase/ formate dehydrogenase bienzymatic system for CO2 capture, utilization and storage

2021 ◽  
Author(s):  
Ryohei Sato ◽  
Yutaka Amao
Keyword(s):  
Carbonic Anhydrase ◽  
Co2 Capture ◽  
Carbon Capture ◽  
Formate Dehydrogenase ◽  
Candida Boidinii ◽  
And Storage

In order to establish carbon capture, utilization, and storage (CCUS) technology, we focused on the system consisting of two different biocatalysts (formate dehydrogenase from Candida boidinii; CbFDH and carbonic anhydrase...

Conversion of CO2 to formate in an electroenzymatic cell using Candida boidinii formate dehydrogenase

2014 ◽  
Vol 102 ◽  
pp. 9-15 ◽  
Author(s):  
Sungrye Kim ◽  
Min Koo Kim ◽  
Sang Hyun Lee ◽  
Sungho Yoon ◽  
Kwang-Deog Jung
Keyword(s):  
Formate Dehydrogenase ◽  
Candida Boidinii

scholarly journals Regulation and Physiological Role of theDAS1 Gene, Encoding Dihydroxyacetone Synthase, in the Methylotrophic Yeast Candida boidinii

1998 ◽  
Vol 180 (22) ◽  
pp. 5885-5890 ◽  
Author(s):  
Yasuyoshi Sakai ◽  
Tomoyuki Nakagawa ◽  
Masayuki Shimase ◽  
Nobuo Kato
Keyword(s):  
Formate Dehydrogenase ◽  
Physiological Role ◽  
Nitrogen Sources ◽  
Host Genome ◽  
Candida Boidinii ◽  
Carbon And Nitrogen Sources ◽  
Gene Encoding ◽  
Carbon And Nitrogen ◽  
Dihydroxyacetone Synthase

ABSTRACT The physiological role of dihydroxyacetone synthase (DHAS) inCandida boidinii was evaluated at the molecular level. TheDAS1 gene, encoding DHAS, was cloned from the host genome, and regulation of its expression by various carbon and nitrogen sources was analyzed. Western and Northern analyses revealed thatDAS1 expression was regulated mainly at the mRNA level. The regulatory pattern of DHAS was similar to that of alcohol oxidase but distinct from that of two other enzymes in the formaldehyde dissimilation pathway, glutathione-dependent formaldehyde dehydrogenase and formate dehydrogenase. The DAS1 gene was disrupted in one step in the host genome (das1Δ strain), and the growth of the das1Δ strain in various carbon and nitrogen sources was compared with that of the wild-type strain. Thedas1Δ strain had completely lost the ability to grow on methanol, while the strain with a disruption of the formate dehydrogenase gene could survive (Y. Sakai et al., J. Bacteriol. 179:4480–4485, 1997). These and other experiments (e.g., those to determine the expression of the gene and the growth ability of thedas1Δ strain on media containing methylamine or choline as a nitrogen source) suggested that DAS1 is involved in assimilation rather than dissimilation or detoxification of formaldehyde in the cells.

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.

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