Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790

Schenk, T; Müller, Rudolf; Mörsberger, F; Otto, Manfred K.; Lingens, Franz

doi:10.1128/jb.171.10.5487-5491.1989

Cited by 54 publications

(32 citation statements)

References 33 publications

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“…ATCC 39723 (Steiert et al 1987), and with cell extracts from Arthrobacter sp. ATCC 33790 (Schenk et al, 1989). The observation that 2,4-DCP is degraded by strain SR3 but not by Flavobacterium sp.…”

Section: Mixed Culture Experimentsmentioning

confidence: 99%

“…ATCC 39723 cells (Steiert et al 1987) or Arthrobacter sp. ATCC 33790 cell extracts (Schenk et al 1989), may indicate differences in substrate specificity, toxicity, or transport among these strains (Resnick and ) of the influent PCP was removed 48 h after PCP was added to the PCP-MS batch Erlenmeyer flasks supplemented with 0.5% (w/v) glucose (Fig. 9), 22.8% (114 mg·l ) in MS flasks with PCP as sole source of carbon and energy.…”

Section: Mixed Culture Experimentsmentioning

confidence: 99%

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Degradation of phenol and chlorophenols by mixed and pure cultures

Murialdo¹,

Fenoglio²,

Haure³

et al. 2004

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The enrichment of mixed cultures for species capable of degrading phenol and chlorophenols, as well as the isolation of pure cultures are investigated. The cultures obtained are capable of degrading phenol and chlorophenols (pentachlorophenol 2,3,5,6 tetrachlorophenol and 2,4,6 trichlorophenol) but not 2,4,5 trichlorophenol. The results suggest the feasibility of the use of toxic chemicals as phenols, hexadecane and other chlorophenols as co-substrates in field decontamination processes. The inhibitory effect of PCP is shown, and the influence of a readily degradable ancillary carbon source on the performance of pure cultures is reported, as well as the preliminary identification of the bacteria that showed higher PCP degrading activity.

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Section: Mixed Culture Experimentsmentioning

confidence: 99%

Section: Mixed Culture Experimentsmentioning

confidence: 99%

Degradation of phenol and chlorophenols by mixed and pure cultures

Murialdo¹,

Fenoglio²,

Haure³

et al. 2004

WSA

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“…and a Flavobacterium sp., the 20 -12 monooxygenases involved in thepara-hydroxylation of PCP . l 220 were shown to be soluble (19,20,32 (4,14). In this paper, we demonstrate that in M. second enzyme(s) for the removal of halogens from halohydroquinones.…”

Section: Discussionmentioning

confidence: 99%

Characterization of aromatic dehalogenases of Mycobacterium fortuitum CG-2

et al. 1992

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Two different dehalogenation enzymes were found in cell extracts ofMycobacteriumfortuitum CG-2. The first enzyme was a halophenol para-hydroxylase, a membrane-associated monooxygenase that required molecular oxygen and catalyzed the para-hydroxylation and dehalogenation of chlorinated, fluorinated, and brominated phenols to the corresponding halogenated hydroquinones. The membrane preparation with this activity was inhibited by cytochrome P-450 inhibitors and also showed an increase in the A4,, caused by CO. The second enzyme hydroxylated and reductively dehalogenated tetrahalohydroquinones to 1,2,4-trihydroxybenzene. This halohydroquinone-dehalogenating enzyme was soluble, did not require oxygen, and was not inhibited by cytochrome P-450 inhibitors.Actinomycetes are a large and variable group of microorganisms occurring in many habitats, where they take part in the degradation of organic material. Many microbial strains degrading various aromatic pollutants have been isolated from this group. Enzymes so far characterized have been reported to be monooxygenases, hydroxylases, or dioxygenases (for a review, see reference 31). Actinomycetes, including those degrading xenobiotic compounds, have also been shown to be environmentally tenacious, making them a potential source of microorganisms for bioremediation (6,18,29,30).Mycobacterium fortuitum CG-2 was isolated from a tetrachloroguaiacol enrichment culture and shown to degrade several chlorinated phenols, guaiacols, and syringols at micromolar levels (15). Pentachlorophenol (PCP) was shown to be mineralized to CO2, and tetrachloro-para-hydroquinone (TeCH) was detected as an initial intermediate. We have shown that the degradation of polychlorophenols, guaiacols, and syringols proceeds through chlorinatedparahydroquinones in three different Rhodococcus chlorophenolicus strains (1,3,12,13,15) and is mediated by a membrane-associated cytochrome P-450 enzyme (28). The product of this para-hydroxylation, TeCH, is further orthohydroxylated by a soluble halohydroquinone dehalogenase (4,14,28).In this paper, we report on the enzymatic dehalogenation of chlorinated, brominated, and fluorinated phenols and hydroquinones by M. fortuitum CG-2 cell fractions. We show that the halogenated phenols were converted to halogenated para-hydroquinones by a membrane-associated cytochrome P-450 enzyme. The halohydroquinones formed by the para-hydroxylation were further dehalogenated by a soluble halohydroquinone dehalogenase. The results show that M. fortuitum CG-2 dehalogenases are similar to those previously described by us for R. chlorophenolicus PCP-1 and CP-2 (3, 4, 14, 15, 28). MATERIALS AND METHODSBacterial strains and culture conditions. M. fortuitum CG-2 (12, 16) was grown in nutrient broth-yeast extract medium (21) in a gyratory shaker at 28°C. Two-day-old cultures were harvested or induced by the addition of increasing amounts (10 to 50 FtM) of PCP at 24-h intervals and then harvested.Cell fractionation. Cells were harvested by centrifugation (3,000 x g, 10 min, 4°C), resus...

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“…In a previous report, we showed the enzymatic conversion of PCP to tetrachlorohydroquinone with PCP dehalogenase from extracts of Arthrobacter sp. strain ATCC 33790 after sucrose density centrifugation (12). Here we describe the results of experiments using labeling with H218O and 1802, performed to elucidate the dehalogenation mechanism of PCP with the PCP dehalogenase from Arthrobacter sp.…”

mentioning

confidence: 99%

“…PCP dehalogenase was prepared by ultracentrifugation as described previously (12). The solution containing dehalogenating activity was washed twice with 50 mM potassium phosphate buffer (pH 7.5) to remove sucrose.…”

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confidence: 99%

Mechanism of enzymatic dehalogenation of pentachlorophenol by Arthrobacter sp. strain ATCC 33790

1990

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Pentachlorophenol (PCP) dehalogenase from Arthrobacter sp. strain ATCC 33790 converts PCP to tetrachlorohydroquinone. In labeling experiments with H(2)18O or 18O2, only with H(2)18O was labeled product found. However, unlabeled tetrachlorohydroquinone became labeled after incubation with the enzyme in H(2)18O. Therefore, distinction between an oxygenolytic or a hydrolytic dehalogenation mechanism for the PCP dehalogenase is not possible.

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Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790

Cited by 54 publications

References 33 publications

Degradation of phenol and chlorophenols by mixed and pure cultures

Degradation of phenol and chlorophenols by mixed and pure cultures

Characterization of aromatic dehalogenases of Mycobacterium fortuitum CG-2

Mechanism of enzymatic dehalogenation of pentachlorophenol by Arthrobacter sp. strain ATCC 33790

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