Cascade enzymatic reactions for efficient carbon sequestration

Xia, Shunxiang; Zhao, Xueyan; Frigo-Vaz, Benjamin; Zheng, Wenyun; Kim, Jungbae; Wang, Ping

doi:10.1016/j.biortech.2015.01.093

Cited by 14 publications

(7 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Exploitation in biotechnological applications has been challenging due to the unfavourable thermodynamics of the carboxylation. Recently, the use of purified isocitrate dehydrogenase for CO 2 fixation was reported [ 111 ]. Carbon fixation was driven thermodynamically by maintaining a low pH, where CO 2 concentrations are highest, and coupling the reaction to aconitase catalysed removal of isocitrate ( 7 ) to produce aconitate.…”

Section: Reviewmentioning

confidence: 99%

“…In order for CO 2 biotransformation to target a broad range of commodity chemicals, the CO 2 -fixing enzymes must be used as part of multi-enzymatic cascades that convert CO 2 through multiple steps [ 111 , 150 ]. Such reactions may be performed in vitro, where the relative amounts of each biocatalyst and the intermediate concentrations during the reaction can be closely monitored and controlled.…”

Section: Reviewmentioning

confidence: 99%

See 1 more Smart Citation

Biocatalysis for the application of CO₂ as a chemical feedstock

Alissandratos¹,

Easton²

2015

Beilstein J. Org. Chem.

View full text Add to dashboard Cite

SummaryBiocatalysts, capable of efficiently transforming CO2 into other more reduced forms of carbon, offer sustainable alternatives to current oxidative technologies that rely on diminishing natural fossil-fuel deposits. Enzymes that catalyse CO2 fixation steps in carbon assimilation pathways are promising catalysts for the sustainable transformation of this safe and renewable feedstock into central metabolites. These may be further converted into a wide range of fuels and commodity chemicals, through the multitude of known enzymatic reactions. The required reducing equivalents for the net carbon reductions may be drawn from solar energy, electricity or chemical oxidation, and delivered in vitro or through cellular mechanisms, while enzyme catalysis lowers the activation barriers of the CO2 transformations to make them more energy efficient. The development of technologies that treat CO2-transforming enzymes and other cellular components as modules that may be assembled into synthetic reaction circuits will facilitate the use of CO2 as a renewable chemical feedstock, greatly enabling a sustainable carbon bio-economy.

show abstract

Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

Biocatalysis for the application of CO₂ as a chemical feedstock

Alissandratos¹,

Easton²

2015

Beilstein J. Org. Chem.

View full text Add to dashboard Cite

show abstract

“…Enzymatic cascade reactions are of great interest in drug discovery. They are sometimes easily conducted with the use of immobilized enzymes (stepwise immobilized enzymes, mixed immobilized enzymes and co-immobilized enzymes) [9][10][11][12], on various supports [13][14][15][16]. The use of immobilized enzymes for the study of enzymatic cascades has already been investigated [9,11,17].…”

Section: Introductionmentioning

confidence: 99%

Monitoring of successive phosphorylations of thymidine using free and immobilized human nucleoside/nucleotide kinases by Flow Injection Analysis with High-Resolution Mass Spectrometry

Ferey

Silva

Colas

et al. 2019

Analytica Chimica Acta

View full text Add to dashboard Cite

Nucleosides and their analogues play a crucial role in the treatment of several diseases including cancers and viral infections. Their therapeutic efficiency depends on their capacity to be converted to the active nucleoside triphosphates form through successive phosphorylation steps catalyzed by nucleoside/nucleotide kinases. It is thus mandatory to develop an easy, rapid, reliable and sensitive enzyme activity tests. In this study, we monitored the three-step phosphorylation of thymidine to thymidine triphosphate respectively by (1) human thymidine kinase 1 (hTK1), (2) human thymidylate kinase (hTMPK) and (3) human nucleoside diphosphate kinase (hNDPK). Free and immobilized kinase activities were characterized by using the Michaelis-Menten kinetic model. Flow Injection Analysis (FIA) with High-Resolution Mass Spectrometry (HRMS) was used as well as capillary electrophoresis (CE) with UV detection. The three-step cascade phosphorylation of thymidine was also monitored. FIA-HRMS allows a sensitive and rapid evaluation of the phosphorylation process. This study proposes simple, rapid, efficient and sensitive methods for enzyme kinetic studies and successive phosphorylation monitoring with immobilized enzymes.

show abstract

“…Compared with chemical absorbent reactions, biological absorption can be proceeding at ambient conditions with high reaction specificity and unparalleled high energy efficiency [1]. Among these carbon fixations, ICDH reaction has attracted wide attention due to its reversibility and comparable high specific activity [2]. By shifting the system Ph instead of temperature, the direction of reaction can be manipulated, realizing the carbon capture and release strategy [3].…”

Section: Introductionmentioning

confidence: 99%

Gas Phase Carbon Dioxide as an Optimum Substrate for Isocitrate Dehydrogenase Reaction

Xia

Veony

2019

E3S Web Conf.

Self Cite

View full text Add to dashboard Cite

As biocatalytic carbon capture has attracted wide attraction due to its high energy efficiency, the preference of carbon species of the reaction is concerned. The self-evolution between carbon species makes the determination of preference a changeling issue. In this study, by comparing the isocitrate dehydrogenase reaction rate profiles with pre-equilibrated and un-equilibrated HCO3--CO2 solutions, gas phase carbon dioxide was believed as the optimum substrate, as it can provide higher reaction rate. During the carbon capture process, the partial pressure of the carbon dioxide affected both the reaction equilibrium and kinetics, while the interfacial area can only determine the reaction rate.

show abstract

Cascade enzymatic reactions for efficient carbon sequestration

Cited by 14 publications

References 16 publications

Biocatalysis for the application of CO₂ as a chemical feedstock

Biocatalysis for the application of CO₂ as a chemical feedstock

Monitoring of successive phosphorylations of thymidine using free and immobilized human nucleoside/nucleotide kinases by Flow Injection Analysis with High-Resolution Mass Spectrometry

Gas Phase Carbon Dioxide as an Optimum Substrate for Isocitrate Dehydrogenase Reaction

Contact Info

Product

Resources

About

Cascade enzymatic reactions for efficient carbon sequestration

Cited by 14 publications

References 16 publications

Biocatalysis for the application of CO2 as a chemical feedstock

Biocatalysis for the application of CO2 as a chemical feedstock

Monitoring of successive phosphorylations of thymidine using free and immobilized human nucleoside/nucleotide kinases by Flow Injection Analysis with High-Resolution Mass Spectrometry

Gas Phase Carbon Dioxide as an Optimum Substrate for Isocitrate Dehydrogenase Reaction

Contact Info

Product

Resources

About

Biocatalysis for the application of CO₂ as a chemical feedstock

Biocatalysis for the application of CO₂ as a chemical feedstock