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Enantioselective Phenol Coupling by Laccases in the Biosynthesis of Fungal Dimeric Naphthopyrones
Author(s) -
Obermaier Sebastian,
Thiele Wiebke,
Fürtges Leon,
Müller Michael
Publication year - 2019
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201903759
Subject(s) - laccase , chemistry , enzyme , atropisomer , stereochemistry , enantioselective synthesis , chirality (physics) , oxidase test , oxidative coupling of methane , axial chirality , phenol , biocatalysis , catechol , selectivity , oxidative phosphorylation , dimer , biochemistry , catalysis , organic chemistry , reaction mechanism , nambu–jona lasinio model , chiral symmetry breaking , physics , quantum mechanics , quark
Biaryl compounds are ubiquitous metabolites that are often formed by dimerization through oxidative phenol coupling. Hindered rotation around the biaryl bond can cause axial chirality. In nature, dimerizations are catalyzed by oxidative enzymes such as laccases. This class of enzymes is known for non‐specific oxidase reactions while inherent enantioselectivity is hitherto unknown. Here, we describe four related fungal laccases that catalyze γ‐naphthopyrone dimerization in a regio‐ and atropselective manner. In vitro assays revealed that three enzymes were highly P ‐selective ( ee >95 %), while one enzyme showed remarkable flexibility. Its selectivity for M ‐ or P ‐configured dimers varied depending on the reaction conditions. For example, a lower enzyme concentration yielded primarily ( P )‐ustilaginoidin A, whereas the M atropisomer was favored at higher concentration. These results demonstrate inherent enantioselectivity in an enzyme class that was previously thought to comprise only non‐selective oxidases.