Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: Enzyme-based stereocontrol

Three cloned enoate, reductases from the old yellow enzyme family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12-Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing a,p-unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity - only the conjugated C=C bond was reduced, while isolated olefins and carbonyl groups remained intact - with excellent stereoselectivities (ees up to > 99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this enzyme-based stereocontrol is caused by subtle differences within the active site geometries.