Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: Role of veratryl alcohol in lignin biodegradation

Valli, K; Wariishi, Hiroyuki; Gold, M H

doi:10.1021/bi00489a005

Title: Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: Role of veratryl alcohol in lignin biodegradation

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Abstract

Lignin peroxidase (LiP), an extracellular heme enzyme from the lignin-degrading fungus Phanerochaete chrysosporium, catalyzes the H{sub 2}O{sub 2}-dependent oxidation of a variety of nonphenolic lignin model compounds. The oxidation of monomethoxylated lignin model compounds, such as anisyl alcohol (AA), and the role of veratryl alcohol (VA) in LiP reactions were studied. AA oxidation reached a maximum at relatively low H{sub 2}O{sub 2} concentrations, beyond which the extent of the reactions decreased. The presence of VA did not affect AA oxidation at low molar ratios of H{sub 2}O{sub 2} to enzyme; however, at ratios above 100, the presence of VA abolished the decrease in AA oxidation. Addition of stoichiometric amounts of AA to LiP compound II (LiPII) resulted in its reduction to the native enzyme at rates that were significantly faster than the spontaneous rate of reduction, indicating that AA and other monomethoxylated aromatics are directly oxidized by LiP, albeit slowly. Under steady-state conditions in the presence of excess H{sub 2}O{sub 2} and VA, a visible spectrum for LiPII was obtained. In contrast, under steady-state conditions in the presence of AA a visible spectrum was obtained for LiPIII*, a noncovalent complex of LiPIII and H{sub 2}O{sub 2}. These results support amore »« less

Authors:

Valli, K; Wariishi, Hiroyuki; Gold, M H ^[1]

Oregon Graduate Institute of Science and Technology, Beaverton (USA)

Publication Date:: Tue Sep 18 00:00:00 EDT 1990

OSTI Identifier:: 5923448

Resource Type:: Journal Article

Journal Name:: Biochemistry; (USA)

Additional Journal Information:: Journal Volume: 29:37; Journal ID: ISSN 0006-2960

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; LIGNIN; BIODEGRADATION; PEROXIDASES; BIOCHEMICAL REACTION KINETICS; ANISYL RADICALS; BIOCHEMISTRY; PHANEROCHAETE; STOICHIOMETRY; SUBSTRATES; VISIBLE SPECTRA; ARYL RADICALS; CARBOHYDRATES; CHEMICAL REACTIONS; CHEMISTRY; DECOMPOSITION; ENZYMES; EUMYCOTA; FUNGI; KINETICS; ORGANIC COMPOUNDS; OXIDOREDUCTASES; PLANTS; POLYSACCHARIDES; RADICALS; REACTION KINETICS; SACCHARIDES; SPECTRA; 550200* - Biochemistry

Citation Formats


                    Valli, K, Wariishi, Hiroyuki, and Gold, M H. Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: Role of veratryl alcohol in lignin biodegradation.  United States: N. p., 1990. 
        Web.  doi:10.1021/bi00489a005.

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                    Valli, K, Wariishi, Hiroyuki, & Gold, M H. Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: Role of veratryl alcohol in lignin biodegradation.  United States.  https://doi.org/10.1021/bi00489a005

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                    Valli, K, Wariishi, Hiroyuki, and Gold, M H. 1990.  
        "Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: Role of veratryl alcohol in lignin biodegradation".  United States.  https://doi.org/10.1021/bi00489a005.

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@article{osti_5923448,

  title        = {Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: Role of veratryl alcohol in lignin biodegradation},

  author       = {Valli, K and Wariishi, Hiroyuki and Gold, M H},

  abstractNote = {Lignin peroxidase (LiP), an extracellular heme enzyme from the lignin-degrading fungus Phanerochaete chrysosporium, catalyzes the H{sub 2}O{sub 2}-dependent oxidation of a variety of nonphenolic lignin model compounds. The oxidation of monomethoxylated lignin model compounds, such as anisyl alcohol (AA), and the role of veratryl alcohol (VA) in LiP reactions were studied. AA oxidation reached a maximum at relatively low H{sub 2}O{sub 2} concentrations, beyond which the extent of the reactions decreased. The presence of VA did not affect AA oxidation at low molar ratios of H{sub 2}O{sub 2} to enzyme; however, at ratios above 100, the presence of VA abolished the decrease in AA oxidation. Addition of stoichiometric amounts of AA to LiP compound II (LiPII) resulted in its reduction to the native enzyme at rates that were significantly faster than the spontaneous rate of reduction, indicating that AA and other monomethoxylated aromatics are directly oxidized by LiP, albeit slowly. Under steady-state conditions in the presence of excess H{sub 2}O{sub 2} and VA, a visible spectrum for LiPII was obtained. In contrast, under steady-state conditions in the presence of AA a visible spectrum was obtained for LiPIII*, a noncovalent complex of LiPIII and H{sub 2}O{sub 2}. These results support a mechanism whereby VA protects the enzyme from inactivation by H{sub 2}O{sub 2}, thus making more enzyme available for the oxidation of recalcitrant substrates, such as AA and probably polymeric lignin. The results do not support a mechanism whereby VA acts as a radical mediator in the LiP oxidation of AA and other monomethoxylated aromatics.},

  doi          = {10.1021/bi00489a005},

  url          = {https://www.osti.gov/biblio/5923448},
  journal      = {Biochemistry; (USA)},

  issn         = {0006-2960},

  number       = ,

  volume       = 29:37,

  place        = {United States},

  year         = {Tue Sep 18 00:00:00 EDT 1990},

  month        = {Tue Sep 18 00:00:00 EDT 1990}

}

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