In vitro enzymatic oxidation of a fluorine-tagged sulfido substrate analogue: A19F NMR investigation
1H-decoupled 19F NMR has been used to monitor the highly regioselective oxidation of a fluorine-tagged thia-fatty acid derivative by castor stearoyl-ACP Δ9 desaturase. The major enzymatic product, after reductive work-up, was identified as 9-fluoro-1-nonanol. This compound could be easily distinguished from substrate and a 9-sulfoxy by-product on the basis of its 19F NMR chemical shift and spiking experiments using authentic standards. Structural assignment of the cleavage product was confirmed by GC-MS analysis of the enzymatic products. Copyright
Tremblay, Amy E.,Buist, Peter H.,Hodgson, Derek,Dawson, Brian,Whittle, Ed,Shanklin, John
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