A mutant strain of Azotobacter sp. GP1 converted 4-chlorophenol to 4-chlorocatechol under cometabolic conditions. Under the same conditions the wild-type strain accumulated a yellow compound, which by chemical and spectroscopic methods was identified as 5-chloro-2-hydroxy-6-oxohexadienoic acid (5-chloro-2-hydroxy-muconic semialdehyde). The structure of this compound indicates a meta-proximal cleavage of 4-chlorocatechol.
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http://dx.doi.org/10.1111/j.1574-6968.1994.tb06678.x | DOI Listing |
Biochim Biophys Acta
June 2001
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, CNRS UMR 8601, Université René Descartes, Paris V, 45 rue des Saints Pères, 75270 Cedex 06, Paris, France.
Burkholderia cepacia strain AC1100 can be induced for the degradation of 2,4,5-trichlorophenol (2,4,5-TCP). We have purified the active enzyme 30-fold to apparent homogeneity with a 44% yield by a two-step chromatographic procedure, and showed that it consists of a single type of subunit of 59 kDa based on SDS-PAGE using Coomassie blue and Sypro staining. This enzyme has no bound prosthetic group but requires exogenous addition of FAD and NADH to perform the dioxygen-dependent hydroxylation in the 4-position of 2,4,6-TCP.
View Article and Find Full Text PDFJ Bacteriol
January 1997
Institut für Mikrobiologie, Universität Hohenheim, Stuttgart, Germany.
The enzyme which catalyzes the dehalogenation of 2,4,6-trichlorophenol (TCP) was purified to apparent homogeneity from an extract of TCP-induced cells of Azotobacter sp. strain GP1. The initial step of TCP degradation in this bacterium is inducible by TCP; no activity was found in succinate-grown cells or in phenol-induced cells.
View Article and Find Full Text PDFAppl Environ Microbiol
July 1995
Hydroxyquinol 1,2-dioxygenase was purified from cells of the soil bacterium Azotobacter sp. strain GP1 grown with 2,4,6-trichlorophenol as the sole source of carbon. The presumable function of this dioxygenase enzyme in the degradative pathway of 2,4,6-trichlorophenol is discussed.
View Article and Find Full Text PDFJ Bacteriol
January 1995
Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino.
The enzyme which cleaves the benzene ring of 6-chlorohydroxyquinol was purified to apparent homogeneity from an extract of 2,4,6-trichlorophenol-grown cells of Streptomyces rochei 303. Like the analogous enzyme from Azotobacter sp. strain GP1, it exhibited a highly restricted substrate specificity and was able to cleave only 6-chlorohydroxyquinol and hydroxyquinol and not catechol, chlorinated catechols, or pyrogallol.
View Article and Find Full Text PDFFEMS Microbiol Lett
February 1994
Institut für Mikrobiologie der Universität Hohenheim, Stuttgart, FRG.
A mutant strain of Azotobacter sp. GP1 converted 4-chlorophenol to 4-chlorocatechol under cometabolic conditions. Under the same conditions the wild-type strain accumulated a yellow compound, which by chemical and spectroscopic methods was identified as 5-chloro-2-hydroxy-6-oxohexadienoic acid (5-chloro-2-hydroxy-muconic semialdehyde).
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