期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 20, 期 2, 页码 395-402出版社
SPRINGER
DOI: 10.1007/s00775-014-1215-5
关键词
Molybdenum; Voltammetry; Enzyme; Chiral sulfoxide
资金
- Australian Research Council [DP120101465]
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.
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