Molecular biology and structure-function of lignin-degrading heme peroxidases

Three peroxidases involved in lignin degradation are produced by white-rot fungi. Lignin peroxidase (LiP) is characterized by oxidation of high redox-potential aromatic compounds (including veratryl alcohol) whereas manganese peroxidase (MnP) requires Mn2+ to complete the catalytic cycle and forms Mn3+ chelates acting as diffusing oxidizers. Pleurotus and Bjerkandera versatile peroxidase (VP) is able to oxidize Mn2+ as well as non-phenolic aromatic compounds, phenols and dyes. Phanerochaete chrysosporium has two gene families including ten LiP-type and three MnP-type genes coding different isoenzymes expressed during secondary metabolism. Two VP genes have been recently cloned from Pleurotus eryngii. Phanerochaete chrysosporium MnP and P. eryngii VP are induced by H2O2, being Mn2+ involved in regulation of their transcript levels. At least eighteen more ligninolytic peroxidase genes have been cloned from other white-rot fungi. Protein sequence comparison reveals that typical MnP from P. chrysosporium and two other fungi (showing a longer C-terminal tail) are separated from other ligninolytic peroxidases, which form two main groups including P. chrysosporium LiP and Pleurotus peroxidases respectively.