Veratryl alcohol-mediated indirect oxidation of pentachlorophenol by lignin peroxidase

Namhyun Chung, Steven D. Aust

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

The oxidation of pentachlorophenol (PCP) by lignin peroxidase (LIP) is characterized by a rapid loss of activity during which time the enzyme is quickly converted to compound III, an inactive form of the enzyme. We investigated the indirect oxidation of PCP by LiP using veratryl alcohol (VA) as a mediator. The oxidation of VA to veratryl aldehyde by LiP was inhibited by PCP. Inhibition was characterized by lag period followed by the same rate of VA oxidation. The lag period before VA oxidation was increased by increasing concentrations of PCP. During the lag period, PCP was oxidized and the extent of PCP oxidation increased with increasing concentrations of VA. The enzyme stayed as compound II during PCP oxidation in the presence of VA, suggesting that VA has a protective role in the LiP catalysis. The kinetics of PCP oxidation in the presence of VA were similar to those of VA oxidation. All these results suggest that PCP is oxidized indirectly via the veratryl alcohol cation radical. 2,3,5,6-Tetrachloro-p-benzoquinone was a stoichiometric product during PCP oxidation in both the presence and the absence of VA. An equivalent amount of inorganic chloride was formed by oxidative 4-dechlorination during PCP oxidation in the presence of VA. The increase in the rate and extent of PCP oxidation by VA results from mediation of PCP oxidation and reversion of inactive compound III to native enzyme, both by the veratryl alcohol cation radical.

Original languageEnglish
Pages (from-to)143-148
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume322
Issue number1
DOIs
Publication statusPublished - 1995 Oct 4
Externally publishedYes

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Pentachlorophenol
Oxidation
Enzymes
veratryl alcohol
lignin peroxidase
Cations
Dechlorination
Catalysis
Aldehydes

Keywords

  • lignin peroxidase
  • mediation
  • pentachlorophenol
  • veratryl alcohol

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Veratryl alcohol-mediated indirect oxidation of pentachlorophenol by lignin peroxidase. / Chung, Namhyun; Aust, Steven D.

In: Archives of Biochemistry and Biophysics, Vol. 322, No. 1, 04.10.1995, p. 143-148.

Research output: Contribution to journalArticle

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AB - The oxidation of pentachlorophenol (PCP) by lignin peroxidase (LIP) is characterized by a rapid loss of activity during which time the enzyme is quickly converted to compound III, an inactive form of the enzyme. We investigated the indirect oxidation of PCP by LiP using veratryl alcohol (VA) as a mediator. The oxidation of VA to veratryl aldehyde by LiP was inhibited by PCP. Inhibition was characterized by lag period followed by the same rate of VA oxidation. The lag period before VA oxidation was increased by increasing concentrations of PCP. During the lag period, PCP was oxidized and the extent of PCP oxidation increased with increasing concentrations of VA. The enzyme stayed as compound II during PCP oxidation in the presence of VA, suggesting that VA has a protective role in the LiP catalysis. The kinetics of PCP oxidation in the presence of VA were similar to those of VA oxidation. All these results suggest that PCP is oxidized indirectly via the veratryl alcohol cation radical. 2,3,5,6-Tetrachloro-p-benzoquinone was a stoichiometric product during PCP oxidation in both the presence and the absence of VA. An equivalent amount of inorganic chloride was formed by oxidative 4-dechlorination during PCP oxidation in the presence of VA. The increase in the rate and extent of PCP oxidation by VA results from mediation of PCP oxidation and reversion of inactive compound III to native enzyme, both by the veratryl alcohol cation radical.

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