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Degradation of 2,4,6‐trichlorophenol via chlorohydroxyquinol in Ralstonia eutropha JMP134 and JMP222
Author(s) -
Padilla Leandro,
Matus Valeria,
Zenteno Pamela,
González Bernardo
Publication year - 2000
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/1521-4028(200008)40:4<243::aid-jobm243>3.0.co;2-d
Subject(s) - ralstonia , chemistry , degradation (telecommunications) , strain (injury) , catabolism , formaldehyde , enzyme , biodegradation , bacteria , biochemistry , organic chemistry , biology , telecommunications , genetics , computer science , anatomy
Abbreviations: 2,4‐D: 2,4‐dichlorophenoxyacetate; 2,4,6‐TCP: 2,4,6‐trichlorophenol; HQ: hydroxy‐quinol; 6‐CHQ: 6‐chlorohydroxyquinol; 2,6‐DCBQ: 2,6‐dichlorobenzoquinone; 2,6‐DCHQ: 2,6‐dichlorohydroxyquinone; CMA: 2‐chloromaleylacetate; MA: maleylacetate; HQDO: hydroxyquinol dioxygenase; MAR: maleylacetate reductase. The aim of this work was to study the catabolic pathway of the pollutant 2,4,6‐trichlorophenol in Ralstonia eutropha JMP134. 2,6‐dichlorohydroquinone was detected as transient intermediate. Enzymatic transformations of 6‐chlorohydroxyquinol to 2‐chloromaleylacetate, and of this compound to maleylacetate were detected in crude extracts. Therefore, the degradation of 2,4,6‐trichlorophenol proceeded through an hydroxyquinol pathway, different from the other chloroaromatic pathways reported in this strain. The same results were observed in two other 2,4,6‐trichlorophenol degrading strains: R. eutropha JMP222, a derivative of strain JMP134 lacking the chlorocatechol catabolism‐encoding pJP4 plasmid, and a river isolate, Ralstonia sp. PZK.