Microbial degradation of lignin: Role of lignin peroxidase, manganese peroxidase, and laccase

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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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Comparison of lignin peroxidase, horseradish peroxidase and laccase in th6 oxidation of methoxybenzenes

Philip J. KERSTEN,* 11 B. KALYANARAMAN,t Kenneth E. HAMMEL,4 Bengt REINHAMMAR§ and T. Kent KIRK*¶ * Forest Products Laboratory, USDA Forest Service, Madison, WI 53705 and Department of Bacteriology, University of Wisconsin, Madison, WI 53706, tNational Biomedical ESR Center, Medical College of Wisconsin, Milwaukee, WI 53226, $Department of Chemistry, SUNY College of Environmental Sciences and F...

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Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.

Lignin peroxidase oxidizes non-phenolic substrates by one electron to give aryl-cation-radical intermediates, which react further to give a variety of products. The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to th...

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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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Crystal structure of lignin peroxidase.

The crystal structure of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium has been determined to 2.6 A resolution by usine multiple isomorphous replacement methods and simulated annealing refinement. Of the 343 residues, residues 3-335 have been accounted for in the electron density map, including four disulfide bonds. The overall three-dimensional structure is very si...

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ژورنال

عنوان ژورنال: Proceedings of the Japan Academy, Series B

سال: 2004

ISSN: 0386-2208,1349-2896

DOI: 10.2183/pjab.80.204