Transformation of 2,4,6-trinitrotoluene by purified xenobiotic reductase B from Pseudomonas fluorescens I-C.

@article{Pak2000TransformationO2,
  title={Transformation of 2,4,6-trinitrotoluene by purified xenobiotic reductase B from Pseudomonas fluorescens I-C.},
  author={Jeong Won Pak and Kyle Knoke and Daniel R. Noguera and Brian G. Fox and Glenn H. Chambliss},
  journal={Applied and environmental microbiology},
  year={2000},
  volume={66 11},
  pages={4742-50}
}
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. XenB catalyzed the reduction of TNT either by hydride addition to the aromatic ring or by nitro group reduction, with the accumulation of various tautomers of the protonated dihydride-Meisenheimer complex of TNT, 2-hydroxylamino-4,6-dinitrotoluene, and 4-hydroxylamino… CONTINUE READING
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