The roles of veratryl alcohol and oxalate in fungal lignin degradation

Laura Schick Zapanta, Ming Tien

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Veratryl alcohol (3,4-dimethoxybenzyl alcohol) and oxalate are secondary metabolites of Phanerochaete chrysosporium and other white-rot fungi. Veratryl alcohol is involved in lignin peroxidase catalysis as a substrate, and oxalate is involved in Mn peroxidase activity in its ability to chelate Mn2+. The role of veratryl alcohol in lignin degradation has been the subject of numerous studies and considerable debate. Several investigators have proposed that veratryl alcohol can act as a redox mediator of lignin degradation. In this mechanism, veratryl alcohol is oxidized by lignin peroxidase to form a cation radical. This cation radical then acts as a diffusible oxidant, mediating the oxidation of compounds that are putatively inaccessible to the lignin peroxidase active site, such as the bulky lignin polymer. Other investigators suggested that the short lifetime of the veratryl alcohol cation radical would make diffusion from the active site unlikely. Still others have suggested that veratryl alcohol is not a mediator at all and that its primary role is protecting lignin peroxidase from inactivation by H2O2. Recent evidence clearly shows that veratryl alcohol does form a cation radical upon oxidation by lignin peroxidase and that it can mediate the oxidation of some substrates. While the possibility of cation radical diffusion exists, it now appears that an enzyme-bound radical would have greater stability. In contrast, diffusible oxidation does play a role in Mn peroxidase activity. Mn peroxidase catalyzes the oxidation of Mn2+ to Mn3+. Mn3+ is a diffusible oxidant and is capable of oxidizing phenolic substrates. Studies have shown that chelating Mn3+ with oxalate enhances its reactivity with its organic substrates. Other investigations have shown that Mn peroxidase activity is stimulated by oxalate. This article summarizes current understanding of the roles veratryl alcohol and oxalate play in the enzymatic degradation of lignin.

Original languageEnglish (US)
Pages (from-to)93-102
Number of pages10
JournalJournal of Biotechnology
Volume53
Issue number2-3
DOIs
StatePublished - Mar 14 1997

Fingerprint

Oxalates
Lignin
manganese peroxidase
Alcohols
Degradation
Cations
Positive ions
Oxidation
Substrates
Oxidants
Catalytic Domain
Research Personnel
veratryl alcohol
Phanerochaete
Metabolites
Chelation
Fungi
Catalysis
Oxidation-Reduction
Polymers

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

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title = "The roles of veratryl alcohol and oxalate in fungal lignin degradation",
abstract = "Veratryl alcohol (3,4-dimethoxybenzyl alcohol) and oxalate are secondary metabolites of Phanerochaete chrysosporium and other white-rot fungi. Veratryl alcohol is involved in lignin peroxidase catalysis as a substrate, and oxalate is involved in Mn peroxidase activity in its ability to chelate Mn2+. The role of veratryl alcohol in lignin degradation has been the subject of numerous studies and considerable debate. Several investigators have proposed that veratryl alcohol can act as a redox mediator of lignin degradation. In this mechanism, veratryl alcohol is oxidized by lignin peroxidase to form a cation radical. This cation radical then acts as a diffusible oxidant, mediating the oxidation of compounds that are putatively inaccessible to the lignin peroxidase active site, such as the bulky lignin polymer. Other investigators suggested that the short lifetime of the veratryl alcohol cation radical would make diffusion from the active site unlikely. Still others have suggested that veratryl alcohol is not a mediator at all and that its primary role is protecting lignin peroxidase from inactivation by H2O2. Recent evidence clearly shows that veratryl alcohol does form a cation radical upon oxidation by lignin peroxidase and that it can mediate the oxidation of some substrates. While the possibility of cation radical diffusion exists, it now appears that an enzyme-bound radical would have greater stability. In contrast, diffusible oxidation does play a role in Mn peroxidase activity. Mn peroxidase catalyzes the oxidation of Mn2+ to Mn3+. Mn3+ is a diffusible oxidant and is capable of oxidizing phenolic substrates. Studies have shown that chelating Mn3+ with oxalate enhances its reactivity with its organic substrates. Other investigations have shown that Mn peroxidase activity is stimulated by oxalate. This article summarizes current understanding of the roles veratryl alcohol and oxalate play in the enzymatic degradation of lignin.",
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The roles of veratryl alcohol and oxalate in fungal lignin degradation. / Zapanta, Laura Schick; Tien, Ming.

In: Journal of Biotechnology, Vol. 53, No. 2-3, 14.03.1997, p. 93-102.

Research output: Contribution to journalArticle

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