caa a22 4500 605507937 CHVBK 20210128100634.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1215-5 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1215-5 Electrochemically mediated enantioselective reduction of chiral sulfoxides [Elektronische Daten] [Kuan-I. Chen, Victoria Challinor, Linda Kielmann, Philip Sharpe, James De Voss, Ulrike Kappler, Alastair McEwan, Paul Bernhardt] The respiratory DMSO reductase from Rhodobacter capsulatus catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide. Herein, we have utilized this Mo enzyme as an enantioselective catalyst to generate optically pure sulfoxides (methyl p-tolyl sulfoxide, methyl phenyl sulfoxide and phenyl vinyl sulfoxide) from racemic starting materials. A hexaaminecobalt coordination compound in its divalent oxidation state was employed as the mediator of electron transfer between the working electrode and DMSO reductase to continually reactivate the enzyme after turnover. In all cases, chiral HPLC analysis of the reaction mixture revealed that the S-sulfoxide was reduced more rapidly leading to enrichment or isolation of the R isomer. Graphical Abstract: SBIC, 2014 Molybdenum nationallicence Voltammetry nationallicence Enzyme nationallicence Chiral sulfoxide nationallicence Chen Kuan-I School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut Challinor Victoria School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut Kielmann Linda School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut Sharpe Philip School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut De Voss James School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut Kappler Ulrike School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut McEwan Alastair School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut Bernhardt Paul School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 395-402 0949-8257 20:2<395 2015 20 775 https://doi.org/10.1007/s00775-014-1215-5 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1215-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Chen Kuan-I School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 700 1- Challinor Victoria School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 700 1- Kielmann Linda School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 700 1- Sharpe Philip School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 700 1- De Voss James School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 700 1- Kappler Ulrike School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 700 1- McEwan Alastair School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 700 1- Bernhardt Paul School of Chemistry and Molecular Biosciences, University of Queensland, 4072, Brisbane, Australia aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 395-402 0949-8257 20:2<395 2015 20 775