Mn-dependent peroxidase from the lignin-degrading white rot fungus Phlebia radiata

Eija Karhunen (Corresponding Author), Anne Kantelinen, Marja-Leena Niku-Paavola

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

A homogeneous Mn-dependent peroxidase (MnP) was purified from the extracellular culture fluid of the lignin-degrading white rot fungus Phlebia radiata by anion exchange chromatography. The enzyme had a molecular weight of 49,000 and pI 3.8. It was a glycoprotein, containing carbohydrate moieties accounting for 10% of the molecular weight. Mn-peroxidase was capable of oxidizing phenolic compounds in the presence of H2O2, whereas the effect on nonphenolic lignin model compounds was insignificant. MnP contained protoporphyrin IX as a prosthetic group. During enzymatic reactions H2O2 converted the native MnP to compound II. Mn2+ was essential in completing the catalytic cycle by returning the enzyme to its native state. The oxidation of ultimate substrates was dependent on superoxide radicals, O2− and probably on Mn3+ generated during the catalytic cycle. MnP exhibited high activity of NADH oxidation without exogenously added H2O2. It was shown to produce H2O2 at the expense of NADH.

Original languageEnglish
Pages (from-to)25-31
JournalArchives of Biochemistry and Biophysics
Volume279
Issue number1
DOIs
Publication statusPublished - 1990
MoE publication typeA1 Journal article-refereed

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manganese peroxidase
Lignin
Fungi
Peroxidase
NAD
Molecular weight
Oxidation
Molecular Weight
Enzymes
Chromatography
Prosthetics
Superoxides
Anions
Extracellular Fluid
Glycoproteins
Carbohydrates
Fluids
lignin peroxidase
Substrates

Cite this

Karhunen, Eija ; Kantelinen, Anne ; Niku-Paavola, Marja-Leena. / Mn-dependent peroxidase from the lignin-degrading white rot fungus Phlebia radiata. In: Archives of Biochemistry and Biophysics. 1990 ; Vol. 279, No. 1. pp. 25-31.
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title = "Mn-dependent peroxidase from the lignin-degrading white rot fungus Phlebia radiata",
abstract = "A homogeneous Mn-dependent peroxidase (MnP) was purified from the extracellular culture fluid of the lignin-degrading white rot fungus Phlebia radiata by anion exchange chromatography. The enzyme had a molecular weight of 49,000 and pI 3.8. It was a glycoprotein, containing carbohydrate moieties accounting for 10{\%} of the molecular weight. Mn-peroxidase was capable of oxidizing phenolic compounds in the presence of H2O2, whereas the effect on nonphenolic lignin model compounds was insignificant. MnP contained protoporphyrin IX as a prosthetic group. During enzymatic reactions H2O2 converted the native MnP to compound II. Mn2+ was essential in completing the catalytic cycle by returning the enzyme to its native state. The oxidation of ultimate substrates was dependent on superoxide radicals, O2− and probably on Mn3+ generated during the catalytic cycle. MnP exhibited high activity of NADH oxidation without exogenously added H2O2. It was shown to produce H2O2 at the expense of NADH.",
author = "Eija Karhunen and Anne Kantelinen and Marja-Leena Niku-Paavola",
year = "1990",
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Mn-dependent peroxidase from the lignin-degrading white rot fungus Phlebia radiata. / Karhunen, Eija (Corresponding Author); Kantelinen, Anne; Niku-Paavola, Marja-Leena.

In: Archives of Biochemistry and Biophysics, Vol. 279, No. 1, 1990, p. 25-31.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Mn-dependent peroxidase from the lignin-degrading white rot fungus Phlebia radiata

AU - Karhunen, Eija

AU - Kantelinen, Anne

AU - Niku-Paavola, Marja-Leena

PY - 1990

Y1 - 1990

N2 - A homogeneous Mn-dependent peroxidase (MnP) was purified from the extracellular culture fluid of the lignin-degrading white rot fungus Phlebia radiata by anion exchange chromatography. The enzyme had a molecular weight of 49,000 and pI 3.8. It was a glycoprotein, containing carbohydrate moieties accounting for 10% of the molecular weight. Mn-peroxidase was capable of oxidizing phenolic compounds in the presence of H2O2, whereas the effect on nonphenolic lignin model compounds was insignificant. MnP contained protoporphyrin IX as a prosthetic group. During enzymatic reactions H2O2 converted the native MnP to compound II. Mn2+ was essential in completing the catalytic cycle by returning the enzyme to its native state. The oxidation of ultimate substrates was dependent on superoxide radicals, O2− and probably on Mn3+ generated during the catalytic cycle. MnP exhibited high activity of NADH oxidation without exogenously added H2O2. It was shown to produce H2O2 at the expense of NADH.

AB - A homogeneous Mn-dependent peroxidase (MnP) was purified from the extracellular culture fluid of the lignin-degrading white rot fungus Phlebia radiata by anion exchange chromatography. The enzyme had a molecular weight of 49,000 and pI 3.8. It was a glycoprotein, containing carbohydrate moieties accounting for 10% of the molecular weight. Mn-peroxidase was capable of oxidizing phenolic compounds in the presence of H2O2, whereas the effect on nonphenolic lignin model compounds was insignificant. MnP contained protoporphyrin IX as a prosthetic group. During enzymatic reactions H2O2 converted the native MnP to compound II. Mn2+ was essential in completing the catalytic cycle by returning the enzyme to its native state. The oxidation of ultimate substrates was dependent on superoxide radicals, O2− and probably on Mn3+ generated during the catalytic cycle. MnP exhibited high activity of NADH oxidation without exogenously added H2O2. It was shown to produce H2O2 at the expense of NADH.

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SN - 0003-9861

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