Abstract
Ligninase is an extracellular peroxidase produced by several species of white-rot fungi. It is able to oxidize methoxylated substrates to radical cation intermediates that can undergo C—H or C—C bond cleavage, thereby providing the basis for the oxidation of veratryl alcohol or degradation of lignin model compounds respectively. In some cases, the radical cation intermediate can act as an oxidant, accepting an electron from a suitable donor. It can thus function as a mediator, causing oxidation in a polymer not immediately accessible to the enzyme. This could be important in the degradation of natural lignocellulose substrates. However, the removal of a single electron by a mediator would leave a radical in the polymer. We propose that oxygen will bind to this radical to generate active oxygen species. This provides a potential mechanism for the auto-oxidation of lignin at a distance from the enzyme. A scheme is presented to account for the observation that ligninase can open the ring of veratryl alcohol.
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