CHED 828 |
| Carrie M. Webber1, Lian Luo2, and Marian T. Stankovich2. (1) Department of Chemistry, Saint Mary's College of California, 1928 Saint Mary's Road, Moraga, CA 94575, (2) Department of Chemistry, University of Minnesota, 207 Pleasant Street S.E, Minneapolis, MN 55455 |
| Enantiomerically pure (2S)-2-fluorooctanoyl-CoA and (2R)-2-fluorooctanoyl-CoA, the fluorinated substrate analogs of medium-chain acyl-CoA dehydrogenase (MCAD), were prepared from a racemic mixture of ethyl 2-fluorooctanoate. Enantiomeric purity of ethyl 2-fluorooctanoate was achieved via lipase-catalyzed hydrolysis and checked using chiral HPLC. The isomers were converted to their CoA derivatives and used to probe the mechanism of MCAD through proton exchange experiments in the presence of enzyme. The extractability of an α-proton was measured by 19F NMR techniques. It was found that the rate constant for the exchange of the α-proton of (2S)-2-fluorooctanoyl-CoA is 2.4x10-2 s-1, while that for (2R)-2-Fluorooctanoyl-CoA is ca. 10 times slower because its α-proton is not properly oriented to be removed by the enzyme. |
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Undergraduate Research Poster Session: Organic Chemistry
2:00 PM-4:00 PM, Monday, March 29, 2004 Anaheim Convention Center -- Hall A, Poster
Division of Chemical Education |