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. 2014 Jan 27;20(5):1403-9.
doi: 10.1002/chem.201303897. Epub 2013 Dec 30.

NAD(P)H-independent asymmetric C=C bond reduction catalyzed by ene reductases by using artificial co-substrates as the hydrogen donor

Christoph K Winkler  1 , Dorina Clay, Marcello Entner, Markus Plank, Kurt Faber
Affiliations

NAD(P)H-independent asymmetric C=C bond reduction catalyzed by ene reductases by using artificial co-substrates as the hydrogen donor

Christoph K Winkler et al. Chemistry. .

Abstract

To develop a nicotinamide-independent single flavoenzyme system for the asymmetric bioreduction of C=C bonds, four types of hydrogen donor, encompassing more than 50 candidates, were investigated. Six highly potent, cheap, and commercially available co-substrates were identified that (under the optimized conditions) resulted in conversions and enantioselectivities comparable with, or even superior to, those obtained with traditional two-enzyme nicotinamide adenine dinucleotide phosphate (NAD(P)H)-recycling systems.

Keywords: alkene reduction; artificial biocatalysis; ene reductases; enzyme catalysis; hydrogen donors.

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Figures

Scheme 1
Scheme 1
Hydrogen-transfer pathways in the bioreduction of C=C bonds activated by an electron-withdrawing group (EWG): indirect hydrogen transfer from a natural hydrogen donor through nicotinamide catalyzed by a dehydrogenase (coupled-enzyme system); nicotinamide-independent direct hydrogen transfer from an artificial hydrogen donor catalyzed by a single ene reductase (coupled-substrate system).
Scheme 2
Scheme 2
Flavoprotein-catalyzed disproportionation of conjugated enones.
Scheme 3
Scheme 3
Screening of four different types of hydrogen donor (1 c–52 c) in the NAD(P)H-independent bioreduction of 4-ketoisophorone (1 a).
Scheme 4
Scheme 4
Co-substrates used as hydrogen donors in the NAD(P)H-independent bioreduction of 4-ketoisophorone (1 a) to form (R)-levodione (1 b) by using OYE1 and XenA enzymes at pH 7.5 and pH 9 (Boc=tert-butoxycarbonyl).
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References

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