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J Biol Chem. 2013 Nov 29;288(48):34767-76. doi: 10.1074/jbc.M113.514521. Epub 2013 Oct 14.

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

Author information

1
From the Institute of Organic Chemistry, University of Freiburg, Albertstrasse 21, 79104 Freiburg.

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.

KEYWORDS:

Cytochrome P450; Fungi; Glycoprotein; Heme; Magnesium; Oxyfunctionalization; Peroxygenase; Polycyclic Aromatic Hydrocarbons

PMID:
24126915
PMCID:
PMC3843090
DOI:
10.1074/jbc.M113.514521
[Indexed for MEDLINE]
Free PMC Article

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