Studies on Nitrobenzene Metabolism by a Comamonas sp. Strain JS7651

Abstract

Funded studies focused on the biodegradation of nitrobenzene by Comamonas sp. strain JS765, which was isolated in Dr. Jim C. Spain's laboratory, Tyndall AFB. The genes encoding the nitrobenzene dioxygenase system were cloned and sequenced from JS765. The nitrobenzene dioxygenase enzyme system shares high amino acid homology with other identified nitroarene dioxygenase enzymes, in particular the 2-nitrotoluene dioxygenase system from Pseudomonas sp. strain JS42. Nitrobenzene dioxygenase was purified to near homogeneity and had characteristics typical of dioxygenase enzymes. The substrate specificity of nitrobenzene dioxygenase was examined by conducting biotransformations. Based on the substrates examined, it appeared that the substrate specificity of nitrobenzene dioxygenase is different from related enzymes. Gene reporter technology was used to examine the transcriptional regulation of nitrobenzene and 2-nitrotoluene dioxygenase from JS765 and JS42, respectively. Results indicate that both dioxygenases are induced in the presence of salicylate and the respective nitroaromatic compound.

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Document Details

Document Type
Technical Report
Publication Date
Nov 29, 2000
Accession Number
ADA385953

Entities

People

  • Daniel J. Lessner
  • David T. Gibson

Organizations

  • University of Iowa

Tags

Communities of Interest

  • Materials and Manufacturing Processes

DTIC Thesaurus Topics

  • Aerobic Bacteria
  • Amino Acids
  • Aromatic Compounds
  • Bioconversion
  • Biodegradation
  • Dna Sequence Analysis
  • Environment
  • Gas Chromatography
  • Genetic Structures
  • Mass Spectrometry
  • Microbiology
  • Nitrotoluenes
  • Salicylates
  • Sequence Analysis
  • Spectra
  • Substrate Specificity
  • Substrates

Fields of Study

  • Biology

Readers

  • Analytical Chemistry
  • Molecular and Cellular Biochemistry