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Results: 5

1.
FIG. 1.

FIG. 1. From: Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723 .

Pentachlorophenol degradation pathway of S. chlorophenolicum ATCC 39723. PcpB, PCP 4-monooxygenase; PcpD, tetrachloro-p-benzoquinone reductase; PcpC, TeCH reductive dehalogenase; PcpA, DiCH 1,2-dioxygenase; PcpE, chloromaleylacetate reductase; TeCH, tetrachloro-p-hydroquinone; TriCH, trichloro-p-hydroquinone; DiCH, 2,6-dichloro-p-hydroquinone.

Yan Huang, et al. J Bacteriol. 2008 December;190(23):7595-7600.
2.
FIG. 5.

FIG. 5. From: Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723 .

Proposed role of PcpF in the PCP degradation pathway. PcpC catalyzes two consecutive steps in PCP degradation. Both PcpC C14S and PcpC-ox catalyze the formation of GS-TriCH and GS-DiCH conjugates. PcpF channels the conjugates back to the PCP degradation pathway. GS-TriCH, glutathionyl-TriCH; GS-DiCH, glutathionyl-DiCH; PcpC-ox, oxidatively damaged PcpC; PcpF, GS-quinol lyase. Other abbreviations are defined in the legend for Fig. 1.

Yan Huang, et al. J Bacteriol. 2008 December;190(23):7595-7600.
3.
FIG. 4.

FIG. 4. From: Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723 .

PCP toxicity to the S. chlorophenolicum wild type and pcpF mutant. The wild type (Wt) and pcpF mutant (PcpF−) were cultured to an optical density at 600 nm of 1 and plated in serial 10-fold dilutions onto mineral agar plates containing glutamate and various PCP concentrations. The plates were incubated at 30°C for 7 days.

Yan Huang, et al. J Bacteriol. 2008 December;190(23):7595-7600.
4.
FIG. 3.

FIG. 3. From: Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723 .

PCP degradation by the S. chlorophenolicum wild type and pcpF mutant. Cells were growing on glutamate, induced with PCP, harvested, washed, and resuspended to an optical density at 600 nm of 0.6 in mineral medium with glutamate (A) and without glutamate (B). Immediately, PCP was added to a target concentration of 100 μM, and its degradations by the wild type (▪) and the pcpF mutant (▴) were measured.

Yan Huang, et al. J Bacteriol. 2008 December;190(23):7595-7600.
5.
FIG. 2.

FIG. 2. From: Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723 .

HPLC chromatograms of sequential reactions of TeCH transformation by PcpC C14S and PcpF. Reactions were carried out in 100 μl of 70 mM KPi buffer (pH 6.5) containing 2 mM ascorbic acid, 10 mM GSH, and 200 μM TeCH. (A) Reaction mixture only. A total of 20 μl of sample was removed, mixed with 20 μl of acetonitrile-acetic acid (9:1), centrifuged, and analyzed by HPLC. (B) Reaction mixture after the first PcpC C14S catalysis. Two microliters of PcpC C14S (ultracentrifuged cell extracts, 27.6 mg/ml) was added to the remaining 80 μl of reaction mixture, which was incubated at 30°C for 2 min and then heated at 65°C for 5 min before HPLC analysis of 20 μl of sample as described above. (C) Reaction mixture after the first PcpF catalysis and heat inactivation. One microliter of PcpF (2 mg/ml) was added to the remaining sample of reaction mixture B, which was incubated at 30°C for 2 min and then heated at 65°C for 10 min before HPLC analysis of 20 μl of sample as described above. (D) Reaction mixture after the second PcpC C14S (1 μl) catalysis and heat inactivation. (E) Reaction mixture after the second PcpF (0.5 μl) catalysis. HPLC data were extracted at 300 nm and exported in ASCII format and analyzed by Microsoft Excel. The chromatograms were separated by adding a constant of 0.005, 0.010, 0.015, 0.020, or 0.025 to the corresponding set of absorption unit (AU) data.

Yan Huang, et al. J Bacteriol. 2008 December;190(23):7595-7600.

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