“…Enzymes catalyze almost all in - vivo reactions with extremely high selectivity. Many kinds of enzymes are commercially available nowadays, and their utilization as catalysts for in - vitro reactions has attracted considerable attention in relation to practical organic syntheses. − In the field of electrochemistry, high selectivity that enzymes possess has been widely utilized in electroorganic syntheses − and amperometric biosensors. − The electrochemical techniques are also useful to investigate mechanisms and kinetics of the enzymatic reactions. − We have developed some kinds of electrochemical reaction systems using enzymes as electrocatalysts, such as reductive fixation of carbon dioxide into organic molecules such as α-oxoglutaric acid and pyruvic acid and electrochemical reduction of carbon dioxide to methanol. , Furthermore, attempts have been made to use alcohol dehydrogenase (ADH), which is known as a stable enzyme, as an electrocatalyst to induce electrochemical conversion of ketone and aldehyde derivatives to the corresponding alcohols. , Recently, synthesis of chiral compounds is gaining popularity, and electrochemi- cal synthesis using enzymes as the electrocatalysts may provide one promising route to achieve this 1 Two electrochemical reduction systems using alcohol dehydrogenase as an electrocatalyst. 2 Time course of production of ( S )-1-phenoxy-2-propanol obtained by adding 3 mmol dm -3 NADPH to 2 mL of phosphate buffer (pH 7.1) containing 2.0 units of ADH (EC 1.1.1.2), 3.0 mmol dm -3 phenoxy-2-propanone, and 3 vol % tert -butyl alcohol which served as a solubilizing agent for the substrate and product.…”
Section: Introductionmentioning
confidence: 99%
“…[16][17][18][19][20][21][22][23][24][25] The electrochemical techniques are also useful to inves-tigate mechanisms and kinetics of the enzymatic reactions. [26][27][28][29] We have developed some kinds of electrochemical reaction systems using enzymes as electrocatalysts, such as reductive fixation of carbon dioxide into organic molecules such as R-oxoglutaric acid 30 and pyruvic acid 31 and electrochemical reduction of carbon dioxide to methanol. 32,33 Furthermore, attempts have been made to use alcohol dehydrogenase (ADH), which is known as a stable enzyme, as an electrocatalyst to induce electrochemical conversion of ketone and aldehyde derivatives to the corresponding alcohols.…”
Asymmetric electroreduction of ketone and aldehyde derivatives was examined for two electrochemical reduction systems using alcohol dehydrogenase (ADH) as an electrocatalyst. The reaction system A is concerned with reduction of substrates catalyzed by ADH coupled with regeneration of cofactors by another enzyme with assistance of methyl viologen as an electron mediator, and the reaction system B is concerned with the use of ADH as the sole enzyme which catalyzes both reduction of substrates and regeneration of cofactors. In the latter case, a redox couple of phenethyl alcohol/acetophenone is used as an electron mediator to induce the reaction. The electrolysis using the system A allowed asymmetric reduction of acetophenone, propiophenone, phenoxy-2-propanone, pyruvic acid, and 2-phenylpropionaldehyde to the corresponding optically active alcohols with the enantiomer excesses (ee) close to 100% and the current efficiencies larger than 92%, and the turnover number of the cofactor higher than 50 was obtained for electrochemical reduction of phenoxy-2-propanone for 30 h. The reaction system B gave 100% ee for reduction of propiophenone, phenoxy-2-propanone, and pyruvic acid. However, the amount of products obtained was very small for reduction of benzoylformic acid, and a low enantiomer excess was obtained for reduction of phenylpropionaldehyde. Discussion is made focusing on what substrates are suitable for asymmetric reduction induced by the reaction system B.
“…Enzymes catalyze almost all in - vivo reactions with extremely high selectivity. Many kinds of enzymes are commercially available nowadays, and their utilization as catalysts for in - vitro reactions has attracted considerable attention in relation to practical organic syntheses. − In the field of electrochemistry, high selectivity that enzymes possess has been widely utilized in electroorganic syntheses − and amperometric biosensors. − The electrochemical techniques are also useful to investigate mechanisms and kinetics of the enzymatic reactions. − We have developed some kinds of electrochemical reaction systems using enzymes as electrocatalysts, such as reductive fixation of carbon dioxide into organic molecules such as α-oxoglutaric acid and pyruvic acid and electrochemical reduction of carbon dioxide to methanol. , Furthermore, attempts have been made to use alcohol dehydrogenase (ADH), which is known as a stable enzyme, as an electrocatalyst to induce electrochemical conversion of ketone and aldehyde derivatives to the corresponding alcohols. , Recently, synthesis of chiral compounds is gaining popularity, and electrochemi- cal synthesis using enzymes as the electrocatalysts may provide one promising route to achieve this 1 Two electrochemical reduction systems using alcohol dehydrogenase as an electrocatalyst. 2 Time course of production of ( S )-1-phenoxy-2-propanol obtained by adding 3 mmol dm -3 NADPH to 2 mL of phosphate buffer (pH 7.1) containing 2.0 units of ADH (EC 1.1.1.2), 3.0 mmol dm -3 phenoxy-2-propanone, and 3 vol % tert -butyl alcohol which served as a solubilizing agent for the substrate and product.…”
Section: Introductionmentioning
confidence: 99%
“…[16][17][18][19][20][21][22][23][24][25] The electrochemical techniques are also useful to inves-tigate mechanisms and kinetics of the enzymatic reactions. [26][27][28][29] We have developed some kinds of electrochemical reaction systems using enzymes as electrocatalysts, such as reductive fixation of carbon dioxide into organic molecules such as R-oxoglutaric acid 30 and pyruvic acid 31 and electrochemical reduction of carbon dioxide to methanol. 32,33 Furthermore, attempts have been made to use alcohol dehydrogenase (ADH), which is known as a stable enzyme, as an electrocatalyst to induce electrochemical conversion of ketone and aldehyde derivatives to the corresponding alcohols.…”
Asymmetric electroreduction of ketone and aldehyde derivatives was examined for two electrochemical reduction systems using alcohol dehydrogenase (ADH) as an electrocatalyst. The reaction system A is concerned with reduction of substrates catalyzed by ADH coupled with regeneration of cofactors by another enzyme with assistance of methyl viologen as an electron mediator, and the reaction system B is concerned with the use of ADH as the sole enzyme which catalyzes both reduction of substrates and regeneration of cofactors. In the latter case, a redox couple of phenethyl alcohol/acetophenone is used as an electron mediator to induce the reaction. The electrolysis using the system A allowed asymmetric reduction of acetophenone, propiophenone, phenoxy-2-propanone, pyruvic acid, and 2-phenylpropionaldehyde to the corresponding optically active alcohols with the enantiomer excesses (ee) close to 100% and the current efficiencies larger than 92%, and the turnover number of the cofactor higher than 50 was obtained for electrochemical reduction of phenoxy-2-propanone for 30 h. The reaction system B gave 100% ee for reduction of propiophenone, phenoxy-2-propanone, and pyruvic acid. However, the amount of products obtained was very small for reduction of benzoylformic acid, and a low enantiomer excess was obtained for reduction of phenylpropionaldehyde. Discussion is made focusing on what substrates are suitable for asymmetric reduction induced by the reaction system B.
“…Especially, in their later work they show, as one of the first groups, the electrochemical addressing of dehydrogenase enzymes without the requirement of any co‐factor. They present the reduction of CO 2 to methanol with methylviologen as an electron shuttle …”
Section: Enzymatic Electrocatalysis For Co2 Reductionmentioning
In the recent decade, CO2 has increasingly been regarded not only as a greenhouse gas but even more as a chemical feedstock for carbon‐based materials. Different strategies have evolved to realize CO2 utilization and conversion into fuels and chemicals. In particular, biological approaches have drawn attention, as natural CO2 conversion serves as a model for many processes. Microorganisms and enzymes have been studied extensively for redox reactions involving CO2. In this review, we focus on monitoring nonliving biocatalyzed reactions for the reduction of CO2 by using enzymes. We depict the opportunities but also challenges associated with utilizing such biocatalysts. Besides the application of enzymes with co‐factors, resembling natural processes, and co‐factor recovery, we also discuss implementation into photochemical and electrochemical techniques.
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