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|Title:||New insights into lignin peroxidase|
|Abstract:||Lignin peroxidase an extracellular haem containing glycoprotein is able to oxidise non-phenolic aromatic compounds with redox potentials exceeding 1.4 V. This enzyme is employed by ligninolytic fungi to degrade the recalcitrant biopolymer lignin, a cell wall constituent of woody plants. Due to its enlarged substrate range in the presence of specific mediators and due to its high redox potential this enzyme has the potentiality for the application in various industrial processes. But, until recently information concerning the binding mode of the substrate with the enzyme was lacking, therefore hampering progress in the elucidation of the catalytic mechanism. The finding of an unprecedented amino acid modification at a surface tryptophan initiated several investigations during the past few years on the role of this residue, which resulted in the identification of two distinct substrate interaction sites in lignin peroxidase. This mini-review summarises the major outcome of these investigations and describes the underlying structural factors that govern substrate interaction and electron transfer in lignin peroxidase.|
|Appears in Collections:||IJC-A Vol.41A(01) [January 2002]|
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