Please use this identifier to cite or link to this item: http://dx.doi.org/10.18419/opus-8019
Authors: Engesser, Karl-Heinrich
Cain, Ronald B.
Knackmuss, Hans-Joachim
Title: Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657
Issue Date: 1988
metadata.ubs.publikation.typ: Zeitschriftenartikel
metadata.ubs.publikation.source: Archives of microbiology 149 (1988), S. 188-197. URL http://dx.doi.org./10.1007/BF00422004
URI: http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-76524
http://elib.uni-stuttgart.de/handle/11682/8036
http://dx.doi.org/10.18419/opus-8019
Abstract: The TOL plasmid-encoded enzymes of the methyl-benzoate pathway in Pseudomonas putida mt-2 cometabolized 3-trifluoromethyl (TFM)-benzoate. Two products, 3-TFM-1,2-dihydroxy-2-hydrobenzoate (3-TFM-DHB) and 2-hydroxy-6-oxo-7,7,7-trifluoro-hepta-2,4-dienoate (7-TFHOD) were identified chemically and by spectroscopic properties. TFM-substituted analogues of the metabolites of the methylbenzoate pathway were generally converted at drastically reduced rates. The catechol-2,3-dioxygenase from Pseudomonas putida showed moderate turnover rates with 3-TFM-catechol. The catechol-1,2-dioxygenase of Rhodococcus rubropertinctus N657 was totally inhibited by 3-TFM-catechol and did not cleave this substrate. Hammett-type analysis showed the catechol-1,2-dioxygenase reaction to be strongly dependent on the electronic nature of the substituents. Electronegative substituents strongly inhibited catechol cleavage. The catechol-2,3-dioxygenase reaction, however, was only moderately sensitive to electronegative substituents.
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