Stereospecific Hydrogen Transfer by NADPH-Enoyl Coenzyme A Reductase to cis-and trans-Isomers of 2-Enoic Acid

Abstract

An enoyl CoA reductase, solubilized from rat liver mitochondria by sonication, catalyzes the reduction of both oct-cis-2-enoyl CoA and its trans isomer in the presence of NADPH as a specific electron donor. The reduction of these two enoates by the reductase resulted in the transfer of hydrogen from the A-side of NADPH. The possible role of the reductase in the β-oxidation pathway of unsaturated fatty acids is discussed.
The identification of oct-cis-2-enoate and the trans isomer by GC-MS and TLC are also described.