Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657.
The TOL plasmid-encoded enzymes of the methylbenzoate 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.
Engesser
K H
KH
Institut für Mikrobiologie der Universität Stuttgart, Federal Republic of Germany.
Cain
R B
RB
Knackmuss
H J
HJ
D001673:Biodegradation, Environmental; D050548:Catechol 1,2-Dioxygenase; D050557:Catechol 2,3-Dioxygenase; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D049308:Dioxygenases; D008401:Gas Chromatography-Mass Spectrometry; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D012240:Rhodococcus / Q000201:enzymology*; D014050:Toluene / Q000031:analogs & derivatives* / Q000378:metabolism
D014050:Toluene; C055606:3-trifluoromethylbenzoate; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase; D050557:Catechol 2,3-Dioxygenase