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100 80 60 Molecules 2020, 25, 3653 Molecules 2020, 25, x FOR PEER REVIEW 10 of 23 10 of 24 40 catalyzes the formaldehyde to CH3OH. Each enzymatic step in the reduction cascade proceeds in the conversion. It is obviou2s0 that the research has presented an increasing tendency, especially in the opposite direction of the natural (reversible) enzyme-catalyzed reaction and requires NADH as the recent 10 years, suggesting more and more attention was paid to the biocatalytic conversion of CO2. electron donor for the rea0ction. 2000 2004 2008 2012 2016 140 120 100 In 1993 and 1994, Yoneyam et al. [104,105] demonstrated that CO2 can be biocatalyzed into CH3OH in a CO2-saturated phosphate buffer solution, in which pyrroloquinoline quinone (or methyl viologen) was used as60 an electron mediator, and formate dehydrogenase, formaldehyde dehydrogenase, and alcohol dehydrogenase were used as biocatalysts. Subsequently, Obert [106] 40 20 at each step. Such a multi-enzyme system was composed of three different dehydrogenases (Figure 6) that catalyze the conver0sion of CO2 to CH3OH in the presence of NADH. In this enzyme cascade, Year Figure 5. Statistical graph of papers using enzymes as catalyst in CO2 conversion published during the past two decades. 80 presented the reduction of CO2 to methanol using three different dehydrogenases in three consequent reductions, in which reduced nicotinamide adenine dinucleotide (NADH) molecules were required 2000 2004 2008 2012 2016 formate dehydrogenase (FDH) catalyzes the conversion of CO2 to formate, formaldehyde dehydrogenase (FaldDH) then catalyzes the formate to formaldehyde and, finally, alcohol dehydrogenase (ADH) catalyzes the formaldehyde to CH3OH. Each enzymatic step in the reduction Figure 5. Statistical graph of papers using enzymes as catalyst in CO2 conversion published during the Figure 5. Statistical graph of papers using enzymes as catalyst in CO2 conversion published during cascapdaestptwroocededcasdiens.theoppositedirectionofthenatural(reversible)enzyme-catalyzedreactionand the past two decades. requires NADH as the electron donor for the reaction. In 1993 and 1994, Yoneyam et al. [104,105] demonstrated that CO2 can be biocatalyzed into CH3OH in a CO2-saturated phosphate buffer solution, in which pyrroloquinoline quinone (or methyl viologen) was used as an electron mediator, and formate dehydrogenase, formaldehyde dehydrogenase, and alcohol dehydrogenase were used as biocatalysts. Subsequently, Obert [106] presented the reduction of CO2 to methanol using three different dehydrogenases in three consequent Year reductions, in which reduced nicotinamide adenine dinucleotide (NADH) molecules were required Figure 6. Biocatalytic transformation pathway of CO to CH OH via stepwise reverse enzymatic Figure 6. Biocatalytic transformation pathway of CO2 to CH3OH via stepwise reverse enzymatic at each step. Such a multi-enzyme system was composed of three different dehydrogenases (Figure catalysis by FDH, F DH, and ADH [106]. catalysis by FDH, FaldDH, and ADH [106]. 6) that catalyze the conversion of CO2 to CH3OH in the presence of NADH. In this enzyme cascade, formate dehydrogenase (FDH) catalyzes the conversion of CO2 to formate, formaldehyde Researchers [107] also compared CO reduction from different sources of FDH, F DH, and ADH 2 ald Researchers [107] also compared CO2 reduction from different sources of FDH, FaldDH, and ADH dehydrogenase (FaldDH) then catalyzes the formate to formaldehyde and, finally, alcohol to gain an in-depth understanding of the multi-enzyme cascade reaction. The formate dehydrogenase to gain an in-depth understanding of the multi-enzyme cascade reaction. The formate dehydrogenase dehydrogenase (ADH) catalyzes the formaldehyde to CH3OH. Each enzymatic step in the reduction (ClFDH), formaldehyde dehydrogenase (BmFaldDH), and alcohol dehydrogenase (YADH) were from (ClFDH), formaldehyde dehydrogenase (BmFaldDH), and alcohol dehydrogenase (YADH) were cascade proceeds in the opposite direction of the natural (reversible) enzyme-catalyzed reaction and Clostridium ljungdahlii, Burkholderia multivorans, and Saccharomyces cerevisiae, respectively. A 500-fold from Clostridium ljungdahlii, Burkholderia multivorans, and Saccharomyces cerevisiae, respectively. A 500- requires NADH as the electron donor for the reaction. increase in total turnover number was observed for the ClFDH–BmFaldDH–YADH cascade system fold increase in total turnover number was observed for the ClFDH–BmFaldDH–YADH cascade compared to the Candida boidinii FDH–Pseudomonas putida FaldDH–YADH system. This is conducive system compared to the Candida boidinii FDH–Pseudomonas putida FaldDH–YADH system. This is to develop an enzyme cascade reaction with higher conversion efficiency. The three dehydrogenases conducive to develop an enzyme cascade reaction with higher conversion efficiency. The three cannotonlybecombinedtoconvertCO intomethanolbutalsocanbeusedindividuallytoconvert 2 dehydrogenases can not only be combined to convert CO2 into methanol but also can be used CO tocorrespondingproductssuchasformateorformaldehyde. 2 individually to convert CO2 to corresponding products such as formate or formaldehyde. Up to now, dehydrogenases including formate (FDH), formaldehyde (FaldDH), and alcohol dehydrogenase (ADH) that are usually used as biocatalysts in CO2 reduction are NAH(P)H dependent. HoweFviegru,rNeA6D.BHioicsaetaxlpyetincstirvaen,safonrdmtahteioenxtpeantshiwveayusoefoCfON2AtoDCHHin3OcrHeavsieadsttheepwcoisetorfeveenrzsyemenaztiycmreaatiction. The recgaetanleyrsaistiboynFeDffiHc,ieFnaldcDyHo,faNndAADD(PH)H[1b06e]c.ame an important criterion for evaluating the biocatalytic reaction and more efforts should be devoted to improving the NAD(P)H yield and reducing the Researchers [107] also compared CO2 reduction from different sources of FDH, FaldDH, and ADH production cost. to gain an in-depth understanding of the multi-enzyme cascade reaction. The formate dehydrogenase The combination of enzymes and photocatalysts for CO2 conversion has attracted increasing (ClFDH), formaldehyde dehydrogenase (BmFaldDH), and alcohol dehydrogenase (YADH) were attention because it makes full use of the abundant energy supply of solar light and high specificity from Clostridium ljungdahlii, Burkholderia multivorans, and Saccharomyces cerevisiae, respectively. A 500- of enzyme catalysis [108–110]. These reactions can be conducted at mild conditions similar to the fold increase in total turnover number was observed for the ClFDH–BmFaldDH–YADH cascade photosynthesis that occurs in plants or certain bacteria. This is also called artificial photosynthesis. system compared to the Candida boidinii FDH–Pseudomonas putida FaldDH–YADH system. This is The combination of electrodes with suitable biological enzymes could minimize the requirement of conducive to develop an enzyme cascade reaction with higher conversion efficiency. The three dehydrogenases can not only be combined to convert CO2 into methanol but also can be used individually to convert CO2 to corresponding products such as formate or formaldehyde. Published papers Published papersPDF Image | Research Progress in Conversion of CO2 to Valuable Fuels
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