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Aromatic hydrocarbon dioxygenases in environmental biotechnology.
Aromatic hydrocarbon dioxygenases have a broad substrate specificity and catalyze enantiospecific reactions with a wide range of substrates and make them attractive synthons for the production of industrially and medically important chiral chemicals. Expand
Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase.
The present study was conducted to provide essential structural information necessary for elucidating the mechanism of action of NDO and found the domain structure and iron coordination of the Rieske domain is very similar to that of the cytochrome bc1 domain. Expand
Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB 9816-4.
The multicomponent enzyme, naphthalene dioxygenase, initiates the metabolism of naphthalene by Pseudomonas putida strains G7 (PpG7) and NCIB 9816-4 (Pp9816-4). The genes involved (nahAaAbAcAd) areExpand
Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli.
The tod-C1C2BAD genes show significant homology to the reported nucleotide sequence for benzene dioxygenase and cis-1,2-dihydroxycyclohexa-3,5-diene dehydrogenase from P. putida 136R-3. Expand
Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo.
The results suggest that indigo formation is due to the combined activities of tryptophanase and naphthalene dioxygenase. Expand
Degradation of trichloroethylene by toluene dioxygenase in whole-cell studies with Pseudomonas putida F1
A series of mutant strains derived from P. putida F1 that are defective in the todC gene, which encodes the oxygenase component of toluene dioxygenase, failed to degrade trichloroethylene and to oxidize indole to indigo, and a spontaneous revertant selected from a tod C culture regained simultaneously the abilities to oxidizing toluenes, to form indigo and to degradetrichlorOethylene. Expand
Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol
Kinetic analyses revealed that 2,3-dioxygenase preparations from toluene-grown cells of Pseudomonas putida catalyzed the stoichiometric oxidation of 3-methylcatechol to 2-hydroxy-6-oxohepta-2,4-dienoate and 3-chlorocatechol were noncompetitive or mixed-type inhibitors of the enzyme. Expand
Microbial degradation of organic compounds.
16 contributions by various authors. Degradative pathways. Chemical characterisation of biodegradation. C1 compounds transformation. Aliphatic compounds. Alcyclic rings. Aromatics hydrocarbons.Expand
Molecular Characterization and Substrate Specificity of Nitrobenzene Dioxygenase from Comamonas sp. Strain JS765
NBDO is the first member of the naphthalene family of Rieske nonheme iron oxygenases reported to oxidize all of the isomers of mono- and dinitrotoluenes with the concomitant release of nitrite. Expand