AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schenzle, A.
Right arrow Articles by Knackmuss, H.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schenzle, A.
Right arrow Articles by Knackmuss, H.-J.
Agricola
Right arrow Articles by Schenzle, A.
Right arrow Articles by Knackmuss, H.-J.

Applied and Environmental Microbiology, June 1999, p. 2317-2323, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Chemoselective Nitro Group Reduction and Reductive Dechlorination Initiate Degradation of 2-Chloro-5-Nitrophenol by Ralstonia eutropha JMP134

Andreas Schenzle,1,2,dagger Hiltrud Lenke,1 Jim C. Spain,3 and Hans-Joachim Knackmuss1,2,*

Fraunhofer-Institut für Grenzflächen- und Bioverfahrenstechnik1 and Institut für Mikrobiologie der Universität Stuttgart,2 D-70569 Stuttgart, Germany, and Armstrong Laboratory, AFRL/MRLQ, Tyndall Air Force Base, Florida 32403-53193

Received 25 November 1998/Accepted 29 March 1999

Ralstonia eutropha JMP134 utilizes 2-chloro-5-nitrophenol as a sole source of nitrogen, carbon, and energy. The initial steps for degradation of 2-chloro-5-nitrophenol are analogous to those of 3-nitrophenol degradation in R. eutropha JMP134. 2-Chloro-5-nitrophenol is initially reduced to 2-chloro-5-hydroxylaminophenol, which is subject to an enzymatic Bamberger rearrangement yielding 2-amino-5-chlorohydroquinone. The chlorine of 2-amino-5-chlorohydroquinone is removed by a reductive mechanism, and aminohydroquinone is formed. 2-Chloro-5-nitrophenol and 3-nitrophenol induce the expression of 3-nitrophenol nitroreductase, of 3-hydroxylaminophenol mutase, and of the dechlorinating activity. 3-Nitrophenol nitroreductase catalyzes chemoselective reduction of aromatic nitro groups to hydroxylamino groups in the presence of NADPH. 3-Nitrophenol nitroreductase is active with a variety of mono-, di-, and trinitroaromatic compounds, demonstrating a relaxed substrate specificity of the enzyme. Nitrosobenzene serves as a substrate for the enzyme and is converted faster than nitrobenzene.

* Corresponding author. Mailing address: Institut für Mikrobiologie der Universität Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany. Phone: (49) 711 685 5487. Fax: (49) 711 685 5725. E-mail: imbhjk{at}po.uni-stuttgart.de.

dagger Present address: DuPont Company, Central Research & Development Dept., E328/B48a Experimental Station, Wilmington, DE 19898.

Applied and Environmental Microbiology, June 1999, p. 2317-2323, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 1999 by the American Society for Microbiology. All rights reserved.