Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium.

A. Andrawis, K. A. Johnson, Ming Tien

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

Ligninase, isolated from the wood-destroying fungus Phanerochaete chrysosporium, catalyzes the oxidation of lignin and lignin-related compounds. Ligninase reacts with H2O2 to form the classical peroxidase intermediates Compounds I and II. We have determined the activation energy of ligninase Compound I formation to be 5.9 kcal/mol. The effect of pH and ionic strength on the rate of ligninase Compound I formation was studied. In contrast to all other peroxidases, no pH effect was observed. This is despite homology of active-site amino acids residues (Tien, M., and Tu, C.-P. D. (1987) Nature 326, 520-523) which are proposed to affect the pH profile of Compound I formation. Ligninase Compound I formation can also be supported by organic peroxides. The second-order rate constants with the organic peroxides are lower, suggesting that H2O2 is the preferred substrate.

Original languageEnglish (US)
Pages (from-to)1195-1198
Number of pages4
JournalThe Journal of biological chemistry
Volume263
Issue number3
StatePublished - Jan 1 1988

Fingerprint

Phanerochaete
Lignin
Peroxides
pH effects
Peroxidases
Ionic strength
Fungi
Osmolar Concentration
Peroxidase
Rate constants
Catalytic Domain
Wood
Activation energy
lignin peroxidase
ligninase
Amino Acids
Oxidation
Substrates

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{b2bac3e7cff34a8f9dd37d827e74194b,
title = "Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium.",
abstract = "Ligninase, isolated from the wood-destroying fungus Phanerochaete chrysosporium, catalyzes the oxidation of lignin and lignin-related compounds. Ligninase reacts with H2O2 to form the classical peroxidase intermediates Compounds I and II. We have determined the activation energy of ligninase Compound I formation to be 5.9 kcal/mol. The effect of pH and ionic strength on the rate of ligninase Compound I formation was studied. In contrast to all other peroxidases, no pH effect was observed. This is despite homology of active-site amino acids residues (Tien, M., and Tu, C.-P. D. (1987) Nature 326, 520-523) which are proposed to affect the pH profile of Compound I formation. Ligninase Compound I formation can also be supported by organic peroxides. The second-order rate constants with the organic peroxides are lower, suggesting that H2O2 is the preferred substrate.",
author = "A. Andrawis and Johnson, {K. A.} and Ming Tien",
year = "1988",
month = "1",
day = "1",
language = "English (US)",
volume = "263",
pages = "1195--1198",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "3",

}

Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium. / Andrawis, A.; Johnson, K. A.; Tien, Ming.

In: The Journal of biological chemistry, Vol. 263, No. 3, 01.01.1988, p. 1195-1198.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium.

AU - Andrawis, A.

AU - Johnson, K. A.

AU - Tien, Ming

PY - 1988/1/1

Y1 - 1988/1/1

N2 - Ligninase, isolated from the wood-destroying fungus Phanerochaete chrysosporium, catalyzes the oxidation of lignin and lignin-related compounds. Ligninase reacts with H2O2 to form the classical peroxidase intermediates Compounds I and II. We have determined the activation energy of ligninase Compound I formation to be 5.9 kcal/mol. The effect of pH and ionic strength on the rate of ligninase Compound I formation was studied. In contrast to all other peroxidases, no pH effect was observed. This is despite homology of active-site amino acids residues (Tien, M., and Tu, C.-P. D. (1987) Nature 326, 520-523) which are proposed to affect the pH profile of Compound I formation. Ligninase Compound I formation can also be supported by organic peroxides. The second-order rate constants with the organic peroxides are lower, suggesting that H2O2 is the preferred substrate.

AB - Ligninase, isolated from the wood-destroying fungus Phanerochaete chrysosporium, catalyzes the oxidation of lignin and lignin-related compounds. Ligninase reacts with H2O2 to form the classical peroxidase intermediates Compounds I and II. We have determined the activation energy of ligninase Compound I formation to be 5.9 kcal/mol. The effect of pH and ionic strength on the rate of ligninase Compound I formation was studied. In contrast to all other peroxidases, no pH effect was observed. This is despite homology of active-site amino acids residues (Tien, M., and Tu, C.-P. D. (1987) Nature 326, 520-523) which are proposed to affect the pH profile of Compound I formation. Ligninase Compound I formation can also be supported by organic peroxides. The second-order rate constants with the organic peroxides are lower, suggesting that H2O2 is the preferred substrate.

UR - http://www.scopus.com/inward/record.url?scp=0024296184&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024296184&partnerID=8YFLogxK

M3 - Article

C2 - 3335539

AN - SCOPUS:0024296184

VL - 263

SP - 1195

EP - 1198

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 3

ER -