| Summary: | This study aims to demonstrate the coordination of oxygen regarding the hemophore HasApf expressed by Escherichia coli cells, which appears to create an unlikely oxygen-activating system in HasA due to the already-coordinated iron. In the asymmetric oxidation of rac-1-(6-methoxynaphthalen-2-yl)ethanol (rac-1) using dissolved oxygen, the signals at g-values of 2.8, 2.22, and 1.72 in the electron spin resonance (ESR) spectra disappeared in conjunction with the promotion of oxoferric (FeIII−O–O−) species in the distal site. These results suggest that the iron of porphyrin/Fe may be oxidized in water, leading to exhibition of greater asymmetric oxidation activity in the promotion of oxoferryl (FeIV=O) species. A ketone (~50% chemical yield) produced from (R)-(−)-sec-alcohol can be desymmetrized by NaBH4 in aqueous medium at 40 °C (>99% enantiomer excess, ee, >90% chemical yield) in the absence of NAD(P). Therefore, HasA can be regenerated via successive asymmetric catalytic events through an incorporated iron electron-transfer system in the presence of oxygen: FeII + O2 → FeIII−O–O− → FeIV=O (oxidizing rac-1) → FeII + H2O. This process is similar to a Fenton reaction. The use of a HasA-catalytic system with an incorporated redox cofactor for asymmetric oxidation overcomes the apparent difficulties in working with pure dehydrogenase enzyme/redox cofactor systems for biotransformations.
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