A novel catabolic activity of Pseudomonas veronii in biotransformation of pentachlorophenol

  title={A novel catabolic activity of Pseudomonas veronii in biotransformation of pentachlorophenol},
  author={In-Hyun Nam and Y.-S. Chang and Hyo-Bong Hong and Y.-E. Lee},
  journal={Applied Microbiology and Biotechnology},
Pseudomonas veronii PH-05, a bacterial strain capable of transforming pentachlorophenol (PCP) to a metabolic intermediate, was isolated by selective enrichment of soil samples from a timber storage yard. Strain PH-05 was shown to be able to grow using PCP as the sole source of carbon and energy. GC-MS analysis showed that the metabolic intermediate was tetrachlorocatechol, which inhibited the growth of this strain. The formation of tetrachlorocatechol during biotransformation was monitored, and… Expand
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A comprehensive overview of bacteria and fungi used for pentachlorophenol biodegradation
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Metabolism of pentachlorophenol by a soil microbe.
  • T. Suzuki
  • Chemistry, Medicine
  • Journal of environmental science and health. Part. B, Pesticides, food contaminants, and agricultural wastes
  • 1977
Results of amino acid analysis of the bacterial cells incubated with PCP-14C showed that radioactive carbon derived fromPCP- 14C was incorporated rapidly into the cell constituents, and that the pattern of 14C-amino acids in thecell constituents was not much different between the 15 minute and 24 hour incubation periods. Expand
Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase
The results clearly demonstrate that PCP is oxidatively converted to TeCH by a monooxygenase-type enzyme from Flavobacterium sp. Expand
Mutational analysis of pcpA and its role in pentachlorophenol degradation by Sphingomonas (Flavobacterium) chlorophenolica ATCC 39723
This work confirms that pcpA is essential for degradation of PCP by S. chlorophenolica ATCC 39723 and suggests that it encodes a protein involved in hydrolytic dehalogenation of 2,6-DiCH, an already established primary metabolite of the PCP catabolic pathway. Expand
Isolation and characterization of Flavobacterium strains that degrade pentachlorophenol.
A comparison between strains in their ability to metabolize PCP showed some strains to be more efficient than others, and evidence suggested the presence of a larger plasmid (greater than 200 kilobases) than previously thought. Expand
Evolution of a metabolic pathway for degradation of a toxic xenobiotic: the patchwork approach.
  • S. Copley
  • Biology, Medicine
  • Trends in biochemical sciences
  • 2000
The pathway for degradation of the xenobiotic pesticide pentachlorophenol in Sphingomonas chlorophenolica probably evolved in the past few decades by the recruitment of enzymes from two otherExpand
PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring‐cleavage dioxygenase
PcpA expressed in Escherichia coli was purified to homogeneity and shown to have novel ring‐cleavage dioxygenase activity in conjunction with hydroquinone derivatives, and converting 2,6‐DCHQ to 2‐chloromaleylacetate. Expand
Production and characterization of the recombinant Sphingomonas chlorophenolica pentachlorophenol 4-monooxygenase.
Rec recombinant PCP4MO was identified as apoprotein with no evidence for a typical flavoprotein spectrum and the catalytic activity could be detected in the presence of FAD. Expand
Metabolism of Halophenols by 2,4,5-trichlorophenoxyacetic acid-degrading Pseudomonas cepacia
Resting cells of 2,4,5-trichlorophenoxyacetic acid-grown Pseudomonas cepacia AC1100 were able to completely and rapidly dechlorinate several chlorine-substituted phenols, includingExpand
In vivo levels of chlorinated hydroquinones in a pentachlorophenol-degrading bacterium
An important part of the explanation for why S. chlorophenolica RA-2 is able to grow on PCP as a sole carbon source is undoubtedly that it can process sufficient carbon for growth without accumulating high levels of toxic intermediates. Expand
Purification and characterization of 2,6-dichloro-p-hydroquinone chlorohydrolase from Flavobacterium sp. strain ATCC 39723
The enzyme converted 2,6-DiCH to 6-chlorohydroxyquinol (6-chloro-1,2,4-trihydroxybenzene), which was easily oxidized by molecular oxygen and hard to detect and was detected only in the presence of a reductase and NADH in the reaction mixture. Expand