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Title: Chemotaxis of Pseudomonas putida toward chlorinated benzoates

Abstract

The chlorinated aromatic acids 3-chlorobenzoate and 4-chlorobenzoate are chemoattractants for Pseudomonas putida PRS2000. These compounds are detected by a chromosomally encoded chemotactic response to benzoate which is inducible by {beta}-ketoadipate, and intermediate of benzoate catabolism. Plasmid pAC27, encoding enzymes for 3-chlorobenzoate degradation, does not appear to carry genes for chemotaxis toward chlorinated compounds.

Authors:
; ;  [1]
  1. (Univ. of Iowa, Iowa City (USA))
Publication Date:
OSTI Identifier:
6639159
Resource Type:
Journal Article
Resource Relation:
Journal Name: Applied and Environmental Microbiology; (USA); Journal Volume: 56:5
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; CHLORINATED AROMATIC HYDROCARBONS; BIOLOGICAL EFFECTS; PSEUDOMONAS; BEHAVIOR; PHYSIOLOGY; AROMATICS; BACTERIA; HALOGENATED AROMATIC HYDROCARBONS; MICROORGANISMS; ORGANIC CHLORINE COMPOUNDS; ORGANIC COMPOUNDS; ORGANIC HALOGEN COMPOUNDS 560300* -- Chemicals Metabolism & Toxicology

Citation Formats

Harwood, C.S., Parales, R.E., and Dispensa, M. Chemotaxis of Pseudomonas putida toward chlorinated benzoates. United States: N. p., 1990. Web.
Harwood, C.S., Parales, R.E., & Dispensa, M. Chemotaxis of Pseudomonas putida toward chlorinated benzoates. United States.
Harwood, C.S., Parales, R.E., and Dispensa, M. 1990. "Chemotaxis of Pseudomonas putida toward chlorinated benzoates". United States. doi:.
@article{osti_6639159,
title = {Chemotaxis of Pseudomonas putida toward chlorinated benzoates},
author = {Harwood, C.S. and Parales, R.E. and Dispensa, M.},
abstractNote = {The chlorinated aromatic acids 3-chlorobenzoate and 4-chlorobenzoate are chemoattractants for Pseudomonas putida PRS2000. These compounds are detected by a chromosomally encoded chemotactic response to benzoate which is inducible by {beta}-ketoadipate, and intermediate of benzoate catabolism. Plasmid pAC27, encoding enzymes for 3-chlorobenzoate degradation, does not appear to carry genes for chemotaxis toward chlorinated compounds.},
doi = {},
journal = {Applied and Environmental Microbiology; (USA)},
number = ,
volume = 56:5,
place = {United States},
year = 1990,
month = 5
}
  • Pseudomonas cells able to degrade biphenyl and chlorinated benzoates were used as a basis of the recognition element in amperometric biosensors. The possibility of detecting biphenyl and chlorinated benzoates in a range of concentrations from 0.002 to 0.3 mM and 0.01 to 1.0 mM, respectively, was shown. The sensors were characterized by wide substrate specificity. Their parameters and the dependence of signals on the measurement conditions (pH of the medium, temperature, salt concentration) were studied. It was suggested that these analyzers can be used in practice for evaluation of the total pool of aromatic xenobiotics available at high concentrations inmore » chemical industry wastes.« less
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  • Metabolism of 21 chlorobiphenyls by the enzymes of the upper biphenyl catabolic pathway encoded by the bph locus of Pseudomonas sp. strain LB400 was investigated by using recombinant strains harboring gene cassettes containing bphABC or bphABCD. The enzymes of the upper pathway were generally able to metabolize mono- and dischlorinated biphenyls but only partially transform most trichlorinated congeners investigated: 14 of 15 mono- and dichlorinated and 2 of 6 trichlorinated congeners were converted into benzoates. All mono- and at leas 8 of 12 dichlorinated congeners were attacked by the bphA-encoded biphenyl dioxygenase virtually exclusively at ortho and meta carbons. Thismore » enzyme exhibited a high degree of selectivity for the aromatic ring to be attacked, with the order or ring preference being non- > ortho- > meta- > para-substituted for mono- and dichlorinated congeners. The influence of the chlorine substitution pattern of the metabolized ring on benzoate formation resembled its influence on the reactivity of initial dioxygenation, suggesting that the rate of benzoate formation may frequently be determined by the rate of initial attack. The absorption spectra of phenylhexadienoates formed correlated with the presence or absence of a chlorine substituent at an ortho position. 24 refs., 3 figs., 2 tabs.« less
  • DNA fragments containing the xylD and xylL genes, which specify the broad-specificity enzymes toluate-1,2-dioxygenase and 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase, respectively, of TOL plasmid pWW0-161 of Pseudomonas putida have previously been cloned in the pBR322 vector plasmid. In this study, Escherichia coli cells containing hybrid plasmids carrying the cloned xylD or xylDL genes quantitatively transformed /sup 14/C-ring- and /sup 14/C-carboxy-labeled benzoate to the pathway intermediates 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid (cis-dihydrodiol) and catechol, respectively. Like P. putida cells, E. coli cells containing the xylD gene transformed a variety of chloro- and hydrocarbon-substituted benzoates. The toluate-1,2-dioxygenase produced in E. coli thus exhibited the broad-substrate-specificity properties ofmore » the enzyme in P. putida. Turnover rates by the enzymes in these two bacteria are compared.« less
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