Single-electron transfer processes and the reaction mechanism of enzymic degradation of lignin
TLDR
Lignin degradation Single‐electron transfer Cα‐Cβ bond cleavage Phanerochaete chrysosporium Peroxidase compound IAbout:
This article is published in FEBS Letters.The article was published on 1985-04-08 and is currently open access. It has received 111 citations till now. The article focuses on the topics: Phanerochaete & Bond cleavage.read more
Citations
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Structure and Action Mechanism of Ligninolytic Enzymes
TL;DR: This review covers the chemical nature of lignin substrates and focuses on the biochemical properties, molecular structures, reaction mechanisms, and related structures/functions of these enzymes.
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Polyhaloporphyrins: Unusual Ligands for Metals and Metal-Catalyzed Oxidations
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Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium
TL;DR: A mechanism based upon the ability of radical cations to function as one‐electron oxidants is described and the role of redox mediators in lignin degradation, and the biological significance of veratryl alcohol as a secondary metabolite of P. chrysosporium are discussed.
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Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase.
TL;DR: These findings support the recent proposition that lignin-degrading enzymes are peroxidases, mediating oxidation of aromatic compounds via aryl cation radicals.
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Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds.
TL;DR: Transient-state kinetic studies reveal that, upon reaction of ligninase with H2O2, spectral changes occur in the Soret region, which, by analogy to previous studies of horseradish peroxidase, are consistent with formation of Compounds I and II.
References
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Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase
Ming Tien,T. Kent Kirk +1 more
TL;DR: An extracellular lignin-degrading enzyme from the basidiomycete Phanerochaete chrysosporium Burdsall was purified to homogeneity by ion-exchange chromatography, finding that it is an oxygenase, unique in its requirement for H(2)O(2).
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Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium Burds.
Ming Tien,T. Kent Kirk +1 more
TL;DR: The extracellular fluid of ligninolytic cultures of the wood-decomposing basidiomycete Phanerochaete chrysosporium Burds contains an enzyme that degrades lignin substructure model compounds as well as spruce and birch lignins.
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Separation and characterization of two extracelluar H2O2-dependent oxidases from ligninolytic cultures of Phanerochaete chrysosporium
TL;DR: Two H2O2‐dependent oxidases found in the extracellular medium of the white rot fungus Phanerochaete chrysosporium were separated by chromatography on blue agarose and an Mn2+‐dependent, lactate‐activated peroxidase was identified.
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An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporium.
TL;DR: An H2O2-requiring enzyme system was found in the extracellular medium of ligninolytic cultures of Phanerochaete chrysosporium and produced ethylene from 2-keto-4-thiomethyl butyric acid and partially degraded 14C-ring labeled lignin.
Related Papers (5)
Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium Burds.
Ming Tien,T. Kent Kirk +1 more
Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase
Ming Tien,T. Kent Kirk +1 more