Disease relevance of Trinitrotoluene

• 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 [1].
• Some Clostridium species may reduce TNT to hydroxylaminodinitrotoluenes, which are then further metabolized [1].
• In TNT exposed humans, the notable toxic manifestations have included aplastic anemia, toxic hepatitis, cataract, hepatomegaly and liver cancer [2].
• Escherichia coli grew aerobically with 2,4,6-trinitrotoluene (TNT) as sole nitrogen source and caused TNT's partial denitration [3].
• Zeta-crystallin catalyzes the reductive activation of 2,4,6-trinitrotoluene to generate reactive oxygen species: a proposed mechanism for the induction of cataracts [4].

Psychiatry related information on Trinitrotoluene

• The immunosensor developed could detect TNT as low as 0.09 ng/ml, within a response time of approximately 22 min [5].

High impact information on Trinitrotoluene

• These engineered receptors can function as biosensors for their new ligands; we also incorporated them into synthetic bacterial signal transduction pathways, regulating gene expression in response to extracellular trinitrotoluene or l-lactate [6].
• 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 [1].
• 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 [1].
• Seeds from transgenic plants were able to germinate and grow in the presence of 1 mM glycerol trinitrate (GTN) or 0.05 mM trinitrotoluene, at concentrations that inhibited germination and growth of wild-type seeds [7].
• This review focuses on recent findings that may be relevant for bioremediation or complete degradation of TNT or picric acid [8].

Chemical compound and disease context of Trinitrotoluene

• Biodegradation of nitro-substituted explosives 2,4,6-trinitrotoluene, hexahydro-1,3,5-trinitro-1,3,5-triazine, and octahydro-1,3,5,7-tetranitro-1,3,5-tetrazocine by a phytosymbiotic Methylobacterium sp. associated with poplar tissues (Populus deltoides x nigra DN34) [9].
• TNT (2,4,6-trinitrotoluene) of explosive grade is highly toxic to marine forms that included fresh water unicellular green algae (Selenastrum capricornutum), tidepool copepods (Tigriopus californicus), and oyster larvae (Crassostrea gigas), and mutagenic to Salmonella typhimurium [10].
• Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase [11].
• The enzymatic transformation of 2,4,6-trinitrotoluene (TNT) by purified XenB, an NADPH-dependent flavoprotein oxidoreductase from Pseudomonas fluorescens I-C, was evaluated by using natural abundance and [U-(14)C]TNT preparations [12].
• Aerobic Growth of Escherichia coli with 2,4,6-Trinitrotoluene (TNT) as the Sole Nitrogen Source and Evidence of TNT Denitration by Whole Cells and Cell-Free Extracts [3].

Biological context of Trinitrotoluene

• A dye-labeled TNT analogue prebound in the antibody binding site quenches the QD photoluminescence via proximity-induced FRET [13].
• We demonstrate the use of luminescent QDs conjugated to antibody fragments to develop solution-phase nanoscale sensing assemblies, based on fluorescence resonance energy transfer (FRET) for the specific detection of the explosive 2,4,6-trinitrotoluene (TNT) in aqueous environments [13].
• Analyses also revealed an oxidative stress response upon TNT exposure [14].
• Neuronal nitric oxide synthase (NNOS) catalyzes one-electron reduction of 2,4,6-trinitrotoluene, resulting in decreased nitric oxide production and increased nNOS gene expression: implication for oxidative stress [15].
• Thus, it is suggested that upregulation of nNOS may represent an acute adaptation to an increase in oxidative stress during exposure to TNT [15].

Anatomical context of Trinitrotoluene

• Multiple assays were performed at flow rates of 2.0, 1.0, 0.50, and 0.25 mL/min using membranes saturated with varying TNT antibody concentrations [16].
• Immobilized cells (115-day-old), sampled from a continuous TNT feeding experiment, mineralized [(14)C]-TNT to a level of 15.3% following a 41-day incubation period in a microcosm [17].
• Plasma membrane dependent reduction of 2,4,6-trinitrotoluene by Phanerochaete chrysosporium [18].
• We propose that oxidative DNA damage in the testis plays a role in reproductive toxicity induced by TNT and other nitroaromatic compounds [19].
• Exposure of bovine aortic endothelial cells (BAECs) to TNT (100 microM) resulted in serine 1179 phosphorylation of endothelial NOS (eNOS) [20].

Associations of Trinitrotoluene with other chemical compounds

• Results indicate that OPR2 is involved in plant metabolism of TNT (11-fold induction), and in oxidative stress when exposed to AOC (7-fold), MOC (9-fold), and RDX (2-fold) [21].
• SiO(2) nanospheres were similarly used to modify glassy carbon electrodes for electrochemical detection of TNT and TNB [22].
• Amperometric TNT biosensor based on the oriented immobilization of a nitroreductase maltose binding protein fusion [23].
• These reactive DESI experiments (reactions accompanying desorption) produce such ions as the chloride and trifluoroacetate adducts of RDX and HMX or the Meisenheimer complex of TNT [24].
• We examined the bioremediation of soils contaminated with the munition compounds 2,4,6-trinitrotoluene (TNT), hexahydro-1,3,5-trinitro-1,3,5-triazine, and octahydro-1,3,5,7-tetranitro-1,3,5,7-tetraazocine by a procedure that produced anaerobic conditions in the soils and promoted the biodegradation of nitroaromatic contaminants [25].

Gene context of Trinitrotoluene

• Although TNT concentrations decreased in both P1 and P2 eluates relative to untreated baseline soil (BL) eluates, a recovery in lymphocyte growth/viability and IL-2 secretion was seen with P2 but not P1 eluates relative to BL eluates [26].
• With a crude enzyme preparation, we found that TNT inhibited the enzyme activity of eNOS in a concentration-dependent manner (IC50 value = 49.4 microM) [27].
• The P. fluorescens gene, xenB, encodes a 37,441-Da monomeric, NAD(P)H-dependent flavoprotein that exhibits fivefold regioselectivity for removal of the central nitro group from NG and that transforms TNT but did not readily react with 2-cyclohexen-1-one [28].
• The P. putida gene, xenA, encodes a 39,702-Da monomeric, NAD(P)H-dependent flavoprotein that removes either the terminal or central nitro groups from NG and that reduces 2-cyclohexen-1-one but did not readily reduce 2,4,6-trinitrotoluene (TNT) [28].
• Under the conditions, however, experiments with the inducible NOS inhibitor aminoguanidine revealed that an adaptive response against hypertension caused by TNT occurs [27].

Analytical, diagnostic and therapeutic context of Trinitrotoluene

• These treatments have been designed to achieve mineralization or reduction of TNT and immobilization of its amino derivatives on humic material [1].
• Multichannel homogeneous immunoassay for detection of 2,4,6-trinitrotoluene (TNT) using a microfabricated capillary array electrophoresis chip [29].
• QD-antibody conjugates were successfully used in fluoroimmunoassays for detection of both a protein toxin (staphylococcal enterotoxin B) and a small molecule (2,4,6-trinitrotoluene) [30].
• Electrochemiluminescence enzyme immunoassays for 2,4,6-trinitrotoluene (TNT) and pentaerythritol tetranitrate (PETN) are described [31].
• The final preparation of TNT reductase showed a single band with a subunit molecular weight of 38 kDa on SDS-PAGE [4].

References