Lignin-degrading peroxidases of Phanerochaete chrysosporium

Danying Cai, Ming Tien

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by which they oxidize substrates also appears to be the similar. pH has a similar effect on lignin peroxidase compound I formation as on HRP or CcP; however, the pKa controlling compound I formation for lignin peroxidase appears to be much lower. Lignin-degrading peroxidases are able to catalyze the oxidation of substrates with high redox potential. This unique ability is consistent with a heme active site of low electron density, which is indicated by high redox potential.

Original languageEnglish (US)
Pages (from-to)79-90
Number of pages12
JournalJournal of Biotechnology
Volume30
Issue number1
DOIs
StatePublished - Jul 1993

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Phanerochaete
Peroxidases
Lignin
Cytochrome-c Peroxidase
manganese peroxidase
Horseradish Peroxidase
Oxidation-Reduction
Substrates
Catalytic Domain
Heme
Carrier concentration
Secondary Metabolism
Basidiomycota
Proteins
Amino Acids
Degradation
Oxidation
Enzymes
Amino Acid Sequence
Manganese

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

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abstract = "Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by which they oxidize substrates also appears to be the similar. pH has a similar effect on lignin peroxidase compound I formation as on HRP or CcP; however, the pKa controlling compound I formation for lignin peroxidase appears to be much lower. Lignin-degrading peroxidases are able to catalyze the oxidation of substrates with high redox potential. This unique ability is consistent with a heme active site of low electron density, which is indicated by high redox potential.",
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Lignin-degrading peroxidases of Phanerochaete chrysosporium. / Cai, Danying; Tien, Ming.

In: Journal of Biotechnology, Vol. 30, No. 1, 07.1993, p. 79-90.

Research output: Contribution to journalArticle

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