453-17-8Relevant articles and documents
Electrochemical Activation of Galactose Oxidase: Mechanistic Studies and Synthetic Applications
Fryszkowska, Anna,Klapars, Artis,Marshall, Nicholas,Ruccolo, Serge,Strotman, Neil A.,Zhang, Shaoguang
, p. 7270 - 7280 (2021/06/30)
The enzyme galactose oxidase (GOase) is a copper radical oxidase that catalyzes the aerobic oxidation of primary alcohols to the aldehydes and has been utilized to that end in large-scale pharmaceutical processes. To maintain its catalytic activity and ensure high substrate conversion, GOase needs to be continuously (re)activated by 1e- oxidation of the constantly formed out-of-cycle species (GOasesemi) to the catalytically active state (GOaseox). In this work, we report an electrochemical activation method for GOase that replaces the previously used expensive horseradish peroxidase activator in a GOase-catalyzed oxidation reaction. First, the formation of GOaseox of a specifically engineered variant via nonenzymatic oxidation of GOasesemi was studied by UV-vis spectroscopy. Second, electrochemical oxidation of GOase by mediators was studied using cyclic voltammetry. The electron-transfer rates between GOase and various mediators at different pH values were determined, showing a dependence on both the redox potential of the mediator and the pH. This observation suggests that the oxidation of GOase by mediators at pH 7-9 likely occurs via a concerted proton-coupled electron-transfer (PCET) mechanism under anaerobic conditions. Finally, this electrochemical GOase activation method was successfully applied to the development of a bioelectrocatalytic GOase-mediated aerobic oxidation of benzyl alcohol derivatives, cinnamyl alcohol, and aliphatic polyols, including the desymmetrizing oxidation of 2-ethynylglycerol, a key step in the biocatalytic cascade used to prepare the promising HIV therapeutic islatravir.
Prebiotic synthesis of 2-deoxy-d-ribose from interstellar building blocks promoted by amino esters or amino nitriles
Steer, Andrew M.,Bia, Nicolas,Smith, David K.,Clarke, Paul A.
supporting information, p. 10362 - 10365 (2017/09/25)
Understanding the prebiotic genesis of 2-deoxy-d-ribose, which forms the backbone of DNA, is of crucial importance to unravelling the origins of life, yet remains open to debate. Here we demonstrate that 20 mol% of proteinogenic amino esters promote the selective formation of 2-deoxy-d-ribose over 2-deoxy-d-threopentose in combined yields of ≥4%. We also demonstrate the first aldol reaction promoted by prebiotically-relevant proteinogenic amino nitriles (20 mol%) for the enantioselective synthesis of d-glyceraldehyde with 6% ee, and its subsequent conversion into 2-deoxy-d-ribose in yields of ≥ 5%. Finally, we explore the combination of these two steps in a one-pot process using 20 mol% of an amino ester or amino nitrile promoter. It is hence demonstrated that three interstellar starting materials, when mixed together with an appropriate promoter, can directly lead to the formation of a mixture of higher carbohydrates, including 2-deoxy-d-ribose.
METHOD FOR PRODUCING CARBOHYDRATES FROM DIHYDROXYACETONE
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Paragraph 00152, (2016/12/26)
The present invention relates to the use of dihydroxyacetone ("DHA") in the preparation of a number of natural and rare carbohydrates. The present invention comprises three stages. In the first stage of the present invention, syngas and formaldehyde are produced from natural gas, biogas, biomass and C02 from industrial plants including electricity generating plants, steel mills, cement factories and bio refineries. In the second stage of the present invention, formaldehyde and syngas from first stage are condensed to produce DHA. In the third stage of the present invention, DHA serves as a starting material for the synthesis of natural and rare carbohydrates using enzymes belonging to isomerase, aldolases, epimerase and transketolase groups.