Mechanism of oxidative C alpha-C beta cleavage of a lignin model dimer by Phanerochaete chrysosporium ligninase. Stoichiometry and involvement of free radicals.
نویسندگان
چکیده
منابع مشابه
Ligninase of Phanerochaete chrysosporium
This study examined the ligninase-catalysed degradation of lignin model compounds representing the arylglycerol ,-aryl ether substructure, which is the dominant one in the lignin polymer. Three dimeric model compounds were used, all methoxylated in the 3and 4-positions of the arylglycerol ring (ring A) and having various substituents in the ,-ether-linked aromatic ring (ring B), so that competi...
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Waste water from a molasses alcoholic fermentation plant (MWW) was treated biologically with Phanerochaete chrysosporium. The ability of this white-rot fungus to degrade the dark colored pigments present in MWW and the consequent decrease the effluent's color was examined. The Optimum concentration of MWW for color removal was determined and set at the ratio of 1:10. The color changes durin...
متن کاملExtracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium.
The US Department of Energy has assembled a high quality draft genome of Phanerochaete chrysosporium, a white rot Basidiomycete capable of completely degrading all major components of plant cell walls including cellulose, hemicellulose and lignin. Hundreds of sequences are predicted to encode extracellular enzymes including an impressive number of oxidative enzymes potentially involved in ligno...
متن کاملNucleotide sequence of a ligninase gene from Phanerochaete chrysosporium.
Lignin biodegradation is catalyzed in part by ligninases, also known as lignin peroxidases (1-4). We have cloned and sequenced the gene encoding ligninase isozyme H8 from the white-rot fungus Phanerochaete chrysosporium. The gene is interrupted by eight introns, ranging in size from 49 to 69 bp, which are distributed throughout the gene. Putative transcriptional control signals (underlined) inc...
متن کاملLignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H(2)O(2)-requiring oxygenase.
An extracellular lignin-degrading enzyme from the basidiomycete Phanerochaete chrysosporium Burdsall was purified to homogeneity by ion-exchange chromatography. The 42,000-dalton ligninase contains one protoheme IX per molecule. It catalyzes, nonstereospecifically, several oxidations in the alkyl side chains of lignin-related compounds: C(alpha)-C(beta) cleavage in lignin-related compounds of t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)39479-6