Wednesday, July 29, 2009 - 8:30 AM
S109
Asymmetric Bioreduction of Aromatic Nitro Compounds and Nitroalkenes with Enoate Reductase and Nitroreductase
Yanto Yanto, Melanie Hall, and Andreas S. Bommarius. School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 311 Ferst Drive, N.W., Atlanta, GA 30332-0100
The use of biocatalysts for the synthesis of enantiopure compounds attracts increasing attention in fine chemistry and pharmaceutical industry. Bioreduction of activated alkenes by enoate reductases is one of the emerging biosynthetic tools in the synthesis of chiral aldehydes, ketones, esters, and nitroalkanes [1]. Nitroreductase activity on aromatic nitro compounds using the same enzymes is also often observed [2]. In this study, we have characterized several enzymes for their reductase activity on various nitro-substituted compounds. High degrees of conversion, along with high regio- and stereo-selectivities were obtained in the reduction of substrates such as 1-nitro-2-phenylpropene. In order to broaden the applicability of these enzymes, we investigated the substrate specificity using wide range of C=C activating groups including aldehyde-, ketone-, imide-, and carboxylic acid- moieties. The study explored the possibilities of reduction of nitro-substituted compounds for efficient synthesis of amines.
[1] R. Stuermer et al. Curr. Opin. Chem. Biol. 2007, 11, 203–213
[2] M. D. Roldan et al., FEMS Microbiol. Rev. 2008, 32, 474-500
See more of Advances in biocatalyst development (emphasis on novel biocatalysts)
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See more of The Annual Meeting and Exhibition 2009 (July 26 - 30, 2009)
See more of Invited Oral Papers
See more of The Annual Meeting and Exhibition 2009 (July 26 - 30, 2009)