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Issue 8, 2012
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Reductive dehalogenation of β-haloacrylic ester derivatives mediated by ene-reductases

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Abstract

The enzymatic bioreduction of β-halo-α,β-unsaturated carboxylic esters proceeded via sequential enzymatic C[double bond, length as m-dash]C reduction—β-elimination to afford saturated carboxylic esters. This novel biodegradation pathway combines the reductive activity of ene-reductases with the spontaneous β-elimination of hydrohalous acid from the unstable (saturated) intermediates. Both enantiomers of methyl 2-chloro-, 2-bromo- and 2-iodopropionate were obtained in good to excellent enantiopurity via enzyme-based stereocontrol using various members of the ‘Old Yellow Enzyme’ family of flavoproteins. Overall, this pathway resembles a reductive dehalogenation of β-halogenated acrylic esters.

Graphical abstract: Reductive dehalogenation of β-haloacrylic ester derivatives mediated by ene-reductases

  • This article is part of the themed collection: Biocatalysis
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Article information


Submitted
10 Feb 2012
Accepted
29 Mar 2012
First published
29 Mar 2012

Catal. Sci. Technol., 2012,2, 1548-1552
Article type
Communication

Reductive dehalogenation of β-haloacrylic ester derivatives mediated by ene-reductases

G. Tasnádi, C. K. Winkler, D. Clay, M. Hall and K. Faber, Catal. Sci. Technol., 2012, 2, 1548
DOI: 10.1039/C2CY20079A

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