Description of a Versatile Peroxidase Involved in the Natural Degradation of Lignin That Has Both Manganese Peroxidase and Lignin Peroxidase Substrate Interaction Sites

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Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: a novel peroxidase activation mechanism.

LiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) instead of the tryptophan conserved in other lignin-degrading peroxidases. Pristine LiP showed a lag period in VA (veratryl alcohol) oxidation. However, VA-LiP (LiP after treatment with H2O2 and VA) lacked this lag, and H2O2-LiP (H2O2-treated LiP) was inactive. MS analyses revealed that VA-LiP in...

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On the interaction of lignin peroxidase with lignin

The mechanism by which lignin peroxidase (Lip) interacts with the lignin polymer is discussed. Veratryl alcohol (Valc), a secondary metabolite of white rot fungi, acts as a cofactor for the enzyme. The Lip-redox cycle is discussed in terms of Marcus theory of electron transfer. It is proposed that reaction of a nucleophile in the active site channel with the incipient Valc'. is an essential eve...

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Lignin Peroxidase Of

Ligninase is a generic name for a group of isozymes that catalyze the oxidative depolymerization of lignin. Although undoubtedly produced by other lignin-degrading fungi, these isozymes to data have been isolated only from the basidiomycete Phanerochaete chrysosporium Burds. 1,2 These ligninases are extracellular and are produced during secondary metabolism, brought about by nutrient starvation...

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Direct interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium.

Binding properties of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium against a synthetic lignin (dehydrogenated polymerizate, DHP) were studied with a resonant mirror biosensor. Among several ligninolytic enzymes, only LiP specifically binds to DHP. Kinetic analysis revealed that the binding was reversible, and that the dissociation equilibrium constant was 330 micro...

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Lignin Peroxidase Compound III

Lignin peroxidase compound III (LiPIII) was prepared via three procedures: (a) ferrous LiP + O2 (LiPIIIa), (b) ferric LiP + 0; (LiPIIIb), and (c) LiP compound II + excess HzOz followed by treatment with catalase (LiPIIIc). LiPIIIa, h, and c each have a Soret maximum at -414 nm and visible hands at 543 and 578 nm. LiPIIIa, b, and c each slowly reverted to native ferric Lip, releasing stoichiomet...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1999

ISSN: 0021-9258

DOI: 10.1074/jbc.274.15.10324