TY - GEN A1 - Piontek, Klaus A1 - Strittmatter, Eric A1 - Ullrich, René A1 - Gröbe, Glenn A1 - Pecyna, Marek J. A1 - Kluge, Martin A1 - Scheibner, Katrin A1 - Hofrichter, Martin A1 - Plattner, Dietmar A. T1 - Structural basis of substrate conversion in a new aromatic peroxygenase: cytochrome P450 functionality with benefits T2 - The Journal of Biological Chemistry N2 - Aromatic peroxygenases (APOs) represent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity and were thus recently assigned a distinct EC classification (EC 1.11.2.1). They catalyze, inter alia, oxyfunctionalization reactions of aromatic and aliphatic hydrocarbons with remarkable regio- and stereoselectivities. When compared with cytochrome P450, APOs appear to be the choice enzymes for oxyfunctionalizations in organic synthesis due to their independence from a cellular environment and their greater chemical versatility. Here, the first two crystal structures of a heavily glycosylated fungal aromatic peroxygenase (AaeAPO) are described. They reveal different pH-dependent ligand binding modes. We model the fitting of various substrates in AaeAPO, illustrating the way the enzyme oxygenates polycyclic aromatic hydrocarbons. Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO. KW - Cytochrome P450 KW - Fungi; Glycoprotein KW - Oxyfunctionalization KW - Polycyclic Aromatic Hydrocarbons KW - Peroxygenase Y1 - 2014 UR - https://opus4.kobv.de/opus4-UBICO/frontdoor/index/index/docId/11645 SN - 1083-351X IS - 288 SP - 34767 EP - 34776 ER -