This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kadiyala, V. Articles by Spain, J. C. Search for Related Content PubMed PubMed Citation Articles by Kadiyala, V. Articles by Spain, J. C. Agricola Articles by Kadiyala, V. Articles by Spain, J. C.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, November 2003, p. 6520-6526, Vol. 69, No. 11
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.11.6520-6526.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Construction of Escherichia coli Strains for Conversion of Nitroacetophenones to ortho-Aminophenols

Air Force Research Laboratory, Tyndall Air Force Base, Florida 32403-5323

Received 20 May 2003/ Accepted 1 September 2003

The predominant bacterial pathway for nitrobenzene (NB) degradation uses an NB nitroreductase and hydroxylaminobenzene (HAB) mutase to form the ring-fission substrate ortho-aminophenol. We tested the hypothesis that constructed strains might accumulate the aminophenols from nitroacetophenones and other nitroaromatic compounds. We constructed a recombinant plasmid carrying NB nitroreductase (nbzA) and HAB mutase A (habA) genes, both from Pseudomonas pseudoalcaligenes JS45, and expressed the enzymes in Escherichia coli JS995. IPTG (isopropyl-ß-D-thiogalactopyranoside)-induced cells of strain JS995 rapidly and stoichiometrically converted NB to 2-aminophenol, 2-nitroacetophenone (2NAP) to 2-amino-3-hydroxyacetophenone (2AHAP), and 3-nitroacetophenone (3NAP) to 3-amino-2-hydroxyacetophenone (3AHAP). We constructed another recombinant plasmid containing the nitroreductase gene (nfs1) from Enterobacter cloacae and habA from strain JS45 and expressed the enzymes in E. coli JS996. Strain JS996 converted NB to 2-aminophenol, 2-nitrotoluene to 2-amino-3-methylphenol, 3-nitrotoluene to 2-amino-4-methylphenol, 4-nitrobiphenyl ether to 4-amino-5-phenoxyphenol, and 1-nitronaphthalene to 2-amino-1-naphthol. In larger-scale biotransformations catalyzed by strain JS995, 75% of the 2NAP transformed was converted to 2AHAP, whereas 3AHAP was produced stoichiometrically from 3NAP. The final yields of the aminophenols after extraction and recovery were >64%. The biocatalytic synthesis of ortho-aminophenols from nitroacetophenones suggests that strain JS995 may be useful in the biocatalytic production of a variety of substituted ortho-aminophenols from the corresponding nitroaromatic compounds.

This article has been cited by other articles:

• Meyer, D., Witholt, B., Schmid, A. (2005). Suitability of Recombinant Escherichia coli and Pseudomonas putida Strains for Selective Biotransformation of m-Nitrotoluene by Xylene Monooxygenase. Appl. Environ. Microbiol. 71: 6624-6632 [Abstract] [Full Text]