Using enzyme inhibition as a high throughput method to measure the enantiomeric excess of a chiral sulfoxide.
[reaction: see text] The enantiomeric excess of methyl p-tolyl sulfoxide can be determined in a high throughput format by measuring its ability to inhibit the alcohol dehydrogenase catalyzed oxidation of ethanol. The two enantiomers of the sulfoxide have very different inhibition constants for the enzyme. Thus, the initial rate of ethanol oxidation in the presence of the sulfoxide is correlated with the sulfoxide enantiomeric excess.
Sprout
Christopher M
CM
Department of Chemistry, Brown University, Providence, Rhode Island 02912, USA.
Seto
Christopher T
CT
D000431:Ethanol / Q000737:chemistry*; D007700:Kinetics; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000037:antagonists & inhibitors*; D013237:Stereoisomerism; D013454:Sulfoxides / Q000032:analysis* / Q000737:chemistry / Q000494:pharmacology; D013997:Time Factors
D013454:Sulfoxides; D000431:Ethanol; D010088:Oxidoreductases