Oxidation mechanism of ligninolytic enzymes involved in the degradation of environmental pollutants

Tünde Mester, Ming Tien

Research output: Contribution to journalArticle

135 Citations (Scopus)

Abstract

White rot fungi are the most significant lignin degraders among the wood inhabiting microorganisms. They degrade lignin by extracellular oxidative enzymes. The ligninolytic enzymes also oxidize various environmental pollutants such as polycyclic aromatic hydrocarbons, chlorophenols, and aromatic dyes. The most ubiquitous ligninolytic enzymes produced by these fungi are lignin peroxidases (LP), manganese peroxidases (MnP), and laccases (phenol oxidases). The peroxidases are heme-containing enzymes having typical catalytic cycles, which are characteristic of other peroxidases as well. One molecule of hydrogen peroxide oxidizes the resting (ferric) enzyme withdrawing two electrons. Then the peroxidase is reduced back in two steps of one electron oxidation in the presence of appropriate reducing substrate. The range of the reducing substrates of the two peroxidases is very different due to their altered substrate binding sites. LP is able to oxidize various aromatic compounds, while MnP oxidizes almost exclusively Mn(II) to Mn(III), which then degrades phenolic compounds. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds. In this paper, the mechanism of pollutant oxidation by ligninolytic enzymes is discussed giving an overview on the recent results of enzyme kinetics and structure. (C) 2000 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)51-59
Number of pages9
JournalInternational Biodeterioration and Biodegradation
Volume46
Issue number1
DOIs
StatePublished - Jul 1 2000

Fingerprint

Environmental Pollutants
Enzymes
manganese peroxidase
enzyme
Peroxidases
oxidation
Degradation
Oxidation
degradation
pollutant
Lignin
lignin
Laccase
Fungi
phenolic compound
substrate
Substrates
Manganese
manganese
Chlorophenols

All Science Journal Classification (ASJC) codes

  • Environmental Science(all)
  • Microbiology

Cite this

@article{cb2ad30d3dc3464abf3fe5431325c063,
title = "Oxidation mechanism of ligninolytic enzymes involved in the degradation of environmental pollutants",
abstract = "White rot fungi are the most significant lignin degraders among the wood inhabiting microorganisms. They degrade lignin by extracellular oxidative enzymes. The ligninolytic enzymes also oxidize various environmental pollutants such as polycyclic aromatic hydrocarbons, chlorophenols, and aromatic dyes. The most ubiquitous ligninolytic enzymes produced by these fungi are lignin peroxidases (LP), manganese peroxidases (MnP), and laccases (phenol oxidases). The peroxidases are heme-containing enzymes having typical catalytic cycles, which are characteristic of other peroxidases as well. One molecule of hydrogen peroxide oxidizes the resting (ferric) enzyme withdrawing two electrons. Then the peroxidase is reduced back in two steps of one electron oxidation in the presence of appropriate reducing substrate. The range of the reducing substrates of the two peroxidases is very different due to their altered substrate binding sites. LP is able to oxidize various aromatic compounds, while MnP oxidizes almost exclusively Mn(II) to Mn(III), which then degrades phenolic compounds. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds. In this paper, the mechanism of pollutant oxidation by ligninolytic enzymes is discussed giving an overview on the recent results of enzyme kinetics and structure. (C) 2000 Elsevier Science Ltd.",
author = "T{\"u}nde Mester and Ming Tien",
year = "2000",
month = "7",
day = "1",
doi = "10.1016/S0964-8305(00)00071-8",
language = "English (US)",
volume = "46",
pages = "51--59",
journal = "International Biodeterioration and Biodegradation",
issn = "0964-8305",
publisher = "Elsevier Limited",
number = "1",

}

Oxidation mechanism of ligninolytic enzymes involved in the degradation of environmental pollutants. / Mester, Tünde; Tien, Ming.

In: International Biodeterioration and Biodegradation, Vol. 46, No. 1, 01.07.2000, p. 51-59.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Oxidation mechanism of ligninolytic enzymes involved in the degradation of environmental pollutants

AU - Mester, Tünde

AU - Tien, Ming

PY - 2000/7/1

Y1 - 2000/7/1

N2 - White rot fungi are the most significant lignin degraders among the wood inhabiting microorganisms. They degrade lignin by extracellular oxidative enzymes. The ligninolytic enzymes also oxidize various environmental pollutants such as polycyclic aromatic hydrocarbons, chlorophenols, and aromatic dyes. The most ubiquitous ligninolytic enzymes produced by these fungi are lignin peroxidases (LP), manganese peroxidases (MnP), and laccases (phenol oxidases). The peroxidases are heme-containing enzymes having typical catalytic cycles, which are characteristic of other peroxidases as well. One molecule of hydrogen peroxide oxidizes the resting (ferric) enzyme withdrawing two electrons. Then the peroxidase is reduced back in two steps of one electron oxidation in the presence of appropriate reducing substrate. The range of the reducing substrates of the two peroxidases is very different due to their altered substrate binding sites. LP is able to oxidize various aromatic compounds, while MnP oxidizes almost exclusively Mn(II) to Mn(III), which then degrades phenolic compounds. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds. In this paper, the mechanism of pollutant oxidation by ligninolytic enzymes is discussed giving an overview on the recent results of enzyme kinetics and structure. (C) 2000 Elsevier Science Ltd.

AB - White rot fungi are the most significant lignin degraders among the wood inhabiting microorganisms. They degrade lignin by extracellular oxidative enzymes. The ligninolytic enzymes also oxidize various environmental pollutants such as polycyclic aromatic hydrocarbons, chlorophenols, and aromatic dyes. The most ubiquitous ligninolytic enzymes produced by these fungi are lignin peroxidases (LP), manganese peroxidases (MnP), and laccases (phenol oxidases). The peroxidases are heme-containing enzymes having typical catalytic cycles, which are characteristic of other peroxidases as well. One molecule of hydrogen peroxide oxidizes the resting (ferric) enzyme withdrawing two electrons. Then the peroxidase is reduced back in two steps of one electron oxidation in the presence of appropriate reducing substrate. The range of the reducing substrates of the two peroxidases is very different due to their altered substrate binding sites. LP is able to oxidize various aromatic compounds, while MnP oxidizes almost exclusively Mn(II) to Mn(III), which then degrades phenolic compounds. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds. In this paper, the mechanism of pollutant oxidation by ligninolytic enzymes is discussed giving an overview on the recent results of enzyme kinetics and structure. (C) 2000 Elsevier Science Ltd.

UR - http://www.scopus.com/inward/record.url?scp=0034232913&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034232913&partnerID=8YFLogxK

U2 - 10.1016/S0964-8305(00)00071-8

DO - 10.1016/S0964-8305(00)00071-8

M3 - Article

AN - SCOPUS:0034232913

VL - 46

SP - 51

EP - 59

JO - International Biodeterioration and Biodegradation

JF - International Biodeterioration and Biodegradation

SN - 0964-8305

IS - 1

ER -