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
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
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 Esteve-Núñez, A.
Right arrow Articles by Ramos, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Esteve-Núñez, A.
Right arrow Articles by Ramos, J. L.

Next Article 

Microbiology and Molecular Biology Reviews, September 2001, p. 335-352, Vol. 65, No. 3
1092-2172/01/$04.00+0   DOI: 10.1128/MMBR.65.3.335-352.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Biological Degradation of 2,4,6-Trinitrotoluene

Abraham Esteve-Núñez, Antonio Caballero, and Juan L. Ramos*

Department of Biochemistry and Molecular and Cellular Biology of Plants, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Cientificas, Apdo Correos 419, E-18008 Granada, Spain

Nitroaromatic compounds are xenobiotics that have found multiple applications in the synthesis of foams, pharmaceuticals, pesticides, and explosives. These compounds are toxic and recalcitrant and are degraded relatively slowly in the environment by microorganisms. 2,4,6-Trinitrotoluene (TNT) is the most widely used nitroaromatic compound. Certain strains of Pseudomonas and fungi can use TNT as a nitrogen source through the removal of nitrogen as nitrite from TNT under aerobic conditions and the further reduction of the released nitrite to ammonium, which is incorporated into carbon skeletons. Phanerochaete chrysosporium and other fungi mineralize TNT under ligninolytic conditions by converting it into reduced TNT intermediates, which are excreted to the external milieu, where they are substrates for ligninolytic enzymes. Most if not all aerobic microorganisms reduce TNT to the corresponding amino derivatives via the formation of nitroso and hydroxylamine intermediates. Condensation of the latter compounds yields highly recalcitrant azoxytetranitrotoluenes. Anaerobic microorganisms can also degrade TNT through different pathways. One pathway, found in Desulfovibrio and Clostridium, involves reduction of TNT to triaminotoluene; subsequent steps are still not known. Some Clostridium species may reduce TNT to hydroxylaminodinitrotoluenes, which are then further metabolized. Another pathway has been described in Pseudomonas sp. strain JLR11 and involves nitrite release and further reduction to ammonium, with almost 85% of the N-TNT incorporated as organic N in the cells. It was recently reported that in this strain TNT can serve as a final electron acceptor in respiratory chains and that the reduction of TNT is coupled to ATP synthesis. In this review we also discuss a number of biotechnological applications of bacteria and fungi, including slurry reactors, composting, and land farming, to remove TNT from polluted soils. These treatments have been designed to achieve mineralization or reduction of TNT and immobilization of its amino derivatives on humic material. These approaches are highly efficient in removing TNT, and increasing amounts of research into the potential usefulness of phytoremediation, rhizophytoremediation, and transgenic plants with bacterial genes for TNT removal are being done.


* Corresponding author. Mailing address: Estación Experimental del Zaidín, C/Profesor Albareda 1, E-18008 Granada, Spain. Phone: 34-958-121011. Fax: 34-958-129600. E-mail: jlramos{at}eez.csic.es.


Microbiology and Molecular Biology Reviews, September 2001, p. 335-352, Vol. 65, No. 3
1092-2172/01/$04.00+0   DOI: 10.1128/MMBR.65.3.335-352.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Carmona, M., Zamarro, M. T., Blazquez, B., Durante-Rodriguez, G., Juarez, J. F., Valderrama, J. A., Barragan, M. J. L., Garcia, J. L., Diaz, E. (2009). Anaerobic Catabolism of Aromatic Compounds: a Genetic and Genomic View. Microbiol. Mol. Biol. Rev. 73: 71-133 [Abstract] [Full Text]  
  • van Dillewijn, P., Wittich, R.-M., Caballero, A., Ramos, J.-L. (2008). Type II Hydride Transferases from Different Microorganisms Yield Nitrite and Diarylamines from Polynitroaromatic Compounds. Appl. Environ. Microbiol. 74: 6820-6823 [Abstract] [Full Text]  
  • Ziganshin, A. M., Gerlach, R., Borch, T., Naumov, A. V., Naumova, R. P. (2007). Production of Eight Different Hydride Complexes and Nitrite Release from 2,4,6-Trinitrotoluene by Yarrowia lipolytica. Appl. Environ. Microbiol. 73: 7898-7905 [Abstract] [Full Text]  
  • Xiao, Y., Zhang, J.-J., Liu, H., Zhou, N.-Y. (2007). Molecular Characterization of a Novel ortho-Nitrophenol Catabolic Gene Cluster in Alcaligenes sp. Strain NyZ215. J. Bacteriol. 189: 6587-6593 [Abstract] [Full Text]  
  • Iwaki, H., Muraki, T., Ishihara, S., Hasegawa, Y., Rankin, K. N., Sulea, T., Boyd, J., Lau, P. C. K. (2007). Characterization of a Pseudomonad 2-Nitrobenzoate Nitroreductase and Its Catabolic Pathway-Associated 2-Hydroxylaminobenzoate Mutase and a Chemoreceptor Involved in 2-Nitrobenzoate Chemotaxis. J. Bacteriol. 189: 3502-3514 [Abstract] [Full Text]  
  • Singh, O. V., Nagaraj, N. S. (2006). Transcriptomics, proteomics and interactomics: unique approaches to track the insights of bioremediation. Brief Funct Genomic Proteomic 4: 355-362 [Abstract] [Full Text]  
  • Keenan, B. G., Leungsakul, T., Smets, B. F., Mori, M.-a., Henderson, D. E., Wood, T. K. (2005). Protein Engineering of the Archetypal Nitroarene Dioxygenase of Ralstonia sp. Strain U2 for Activity on Aminonitrotoluenes and Dinitrotoluenes through Alpha-Subunit Residues Leucine 225, Phenylalanine 350, and Glycine 407. J. Bacteriol. 187: 3302-3310 [Abstract] [Full Text]  
  • Williams, R. E., Rathbone, D. A., Scrutton, N. S., Bruce, N. C. (2004). Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins. Appl. Environ. Microbiol. 70: 3566-3574 [Abstract] [Full Text]  
  • Kaplan, C. W., Kitts, C. L. (2004). Bacterial Succession in a Petroleum Land Treatment Unit. Appl. Environ. Microbiol. 70: 1777-1786 [Abstract] [Full Text]  
  • Haynes, C. A., Koder, R. L., Miller, A.-F., Rodgers, D. W. (2002). Structures of Nitroreductase in Three States. EFFECTS OF INHIBITOR BINDING AND REDUCTION. J. Biol. Chem. 277: 11513-11520 [Abstract] [Full Text]