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J. Bacteriol., 01 1995, 307-311, Vol 177, No. 2
I Tomasi, I Artaud, Y Bertheau and D Mansuy
Resting cells of 2,4,5-trichlorophenoxyacetic acid-grown Pseudomonas
cepacia AC1100 metabolize both dichlorophenols, such as 2,4-
dichlorophenol, 2,6-dichlorophenol, 3,4-dichlorophenol, and 3,5-
dichlorophenol, and more highly substituted phenols, such as 2,4,6-
trichlorophenol and pentachlorophenol, to the corresponding
chlorohydroquinones. The first hydroxylation occurs in the para position of
the phenol regardless of whether this position is replaced by a chlorine
substituent. The first evidence leading to the characterization of
para-hydroxylase as a flavin-containing enzyme is provided by the
inhibitory effect of methimazole, an alternate substrate for this
monooxygenase, on the degradative ability of the strain. In a second step,
with tetrachlorohydroquinone, trichlorohydroxyquinone was isolated and
completely characterized. Trichlorohydroxyquinone was also obtained from
tetrachloroquinone. Incubation of the cells in the presence of an external
source of NADPH prevents the further degradation of
tetrachlorohydroquinone, suggesting that the quinone derived from the
two-electron oxidation of the hydroquinone is more likely the substrate for
the second hydroxylation.
Copyright © 1995, American Society for Microbiology
Metabolism of polychlorinated phenols by Pseudomonas cepacia AC1100: determination of the first two steps and specific inhibitory effect of methimazole
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques Associe an CNRS, URA 400, Universite Rene Descartes, Paris, France.
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