Structural basis of substrate conversion in a new aromatic peroxygenase: cytochrome P450 functionality with benefits.

Abstract

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.

DOI: 10.1074/jbc.M113.514521
0501002014201520162017
Citations per Year

105 Citations

Semantic Scholar estimates that this publication has 105 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Piontek2013StructuralBO, title={Structural basis of substrate conversion in a new aromatic peroxygenase: cytochrome P450 functionality with benefits.}, author={Klaus Piontek and Eric F. Strittmatter and Ren{\'e} Ullrich and Glenn Gr{\"{o}be and Marek Jan Pecyna and Martin G. Kluge and Katrin Scheibner and Martin Hofrichter and Dietmar A. Plattner}, journal={The Journal of biological chemistry}, year={2013}, volume={288 48}, pages={34767-76} }