In vitro enzymatic oxidation of a fluorine-tagged sulfido substrate analogue: a 19F 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 delta9 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.
Tremblay
Amy E
AE
Department of Chemistry, Carleton University, 1125 Colonel By Drive, Ottawa, Ontario, Canada K1S 5B6.
Buist
Peter H
PH
Hodgson
Derek
D
Dawson
Brian
B
Whittle
Ed
E
Shanklin
John
J
D005227:Fatty Acids / Q000737:chemistry*; D005233:Fatty Alcohols / Q000032:analysis*; D005461:Fluorine / Q000737:chemistry*; D005462:Fluorine Radioisotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010084:Oxidation-Reduction; D013230:Stearoyl-CoA Desaturase / Q000737:chemistry*; D013440:Sulfides / Q000737:chemistry
C522468:9-fluoro-1-nonanol; D005227:Fatty Acids; D005233:Fatty Alcohols; D005462:Fluorine Radioisotopes; D013440:Sulfides; D005461:Fluorine; D013230:Stearoyl-CoA Desaturase