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http://dx.doi.org/10.18419/opus-8019
Autor(en): | Engesser, Karl-Heinrich Cain, Ronald B. Knackmuss, Hans-Joachim |
Titel: | Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657 |
Erscheinungsdatum: | 1988 |
Dokumentart: | Zeitschriftenartikel |
Erschienen in: | 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 |
Zusammenfassung: | 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. |
Enthalten in den Sammlungen: | 15 Fakultätsübergreifend / Sonstige Einrichtung |
Dateien zu dieser Ressource:
Datei | Beschreibung | Größe | Format | |
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eng29.pdf | 3,04 MB | Adobe PDF | Öffnen/Anzeigen |
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