Lignin Peroxidase

Lignin peroxidase, secreted by the white-rot fungus Phanerochaete chrysosporium in response to nutrient deprivation, catalyzes the H2O2-dependent oxidation of non-phenolic aromatic substrates. The present report summarizes the kinetic and structural characteristics of lignin peroxidase isozymes. Our results indicate that the active site of lignin peroxidase is more electron deficient than other peroxidases. As a result, the redox potential of the heme active site is higher, the heme active site is more reactive and the oxycomplex is more stable than that of other peroxidases. Also discussed is the heme-linked ionization of lignin peroxidase.