Accession Number : ADA303643
Title : Biodegradation of Nitroaromatic Compounds.
Descriptive Note : Final rept. 1 Nov 92-31 Oct 95,
Corporate Author : IOWA UNIV IOWA CITY DEPT OF MICROBIOLOGY
Personal Author(s) : Gibson, David T.
PDF Url : ADA303643
Report Date : 31 OCT 1995
Pagination or Media Count : 12
Abstract : Pseudomonas sp. strain Js42 catalyzes the oxidative removal of nitrite from 2-nitro- toluene to form 3-methylcatechol. This reaction is catalyzed by a multicomponent enzyme system designated 2-nitrotoluene 2,3-dioxygenase. The ferredoxin 2NT component of the dioxygenase system was purified and characterized. It is a Rieske 2Fe-2S protein with properties similar to the isofunctional ferredoxins in other multicomponent dioxygenase systems. The genes encoding the reductase, ferredoxin and terminal oxygenase components of 2-nitrotoluene dioxygenase were cloned and their nucleotide sequences determined. The predicted amino acid sequences of the th%ee protein components showed significant identity to the sequences of the isofunctional components in naphthalene dioxygenase. However, there were significant differences in the substrate specificities of the two enzymes. The gene encoding catechol 2,3- dioxygenase in a nitrobenzene-degrading Comamonas strain was cloned and expressed in H. Coli. The results to date represent the first purification and characterization of an enzyme system that can oxidatively remove nitro substituents from the benzene nucleus.
Descriptors : *OXIDATION, *STRAINS(BIOLOGY), *AROMATIC COMPOUNDS, *BIODEGRADATION, *NITROGEN COMPOUNDS, *PSEUDOMONAS, REMOVAL, ENZYMES, SUBSTRATES, SEQUENCES, ESCHERICHIA COLI, OXYGEN, CODING, PURIFICATION, GENES, CLONES, AMINO ACIDS, NUCLEOTIDES, TOLUENES, FERREDOXIN, NITRITES.
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE