Regioselective para‐Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase

The utilization of CO2 as a carbon source for organic synthesis meets the urgent demand for more sustainability in the production of chemicals. Herein, we report on the enzyme‐catalyzed para‐carboxylation of catechols, employing 3,4‐dihydroxybenzoic acid decarboxylases (AroY) that belong to the UbiD...

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Published in:Angewandte Chemie International Edition 2017-10, Vol.56 (44), p.13893-13897
Main Authors: Payer, Stefan E., Marshall, Stephen A., Bärland, Natalie, Sheng, Xiang, Reiter, Tamara, Dordic, Andela, Steinkellner, Georg, Wuensch, Christiane, Kaltwasser, Susann, Fisher, Karl, Rigby, Stephen E. J., Macheroux, Peter, Vonck, Janet, Gruber, Karl, Faber, Kurt, Himo, Fahmi, Leys, David, Pavkov‐Keller, Tea, Glueck, Silvia M.
Format: Article
Language:English
Subjects:
biocatalysis
Carbon dioxide
Carbon sources
Carboxylation
Catechol
catechols
Communication
Communications
Crystal structure
Decarboxylation
Dihydroxybenzoic acid
Enzymes
Flavin mononucleotide
prenylated FMN
Reaction mechanisms
Regioselectivity
Substrates
Sustainability
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Summary:The utilization of CO2 as a carbon source for organic synthesis meets the urgent demand for more sustainability in the production of chemicals. Herein, we report on the enzyme‐catalyzed para‐carboxylation of catechols, employing 3,4‐dihydroxybenzoic acid decarboxylases (AroY) that belong to the UbiD enzyme family. Crystal structures and accompanying solution data confirmed that AroY utilizes the recently discovered prenylated FMN (prFMN) cofactor, and requires oxidative maturation to form the catalytically competent prFMNiminium species. This study reports on the in vitro reconstitution and activation of a prFMN‐dependent enzyme that is capable of directly carboxylating aromatic catechol substrates under ambient conditions. A reaction mechanism for the reversible decarboxylation involving an intermediate with a single covalent bond between a quinoid adduct and cofactor is proposed, which is distinct from the mechanism of prFMN‐associated 1,3‐dipolar cycloadditions in related enzymes. Biocatalytic CO2 fixation: 3,4‐Dihydroxybenzoic acid decarboxylases are shown to catalyze the regioselective para‐carboxylation of the aromatic core of catechols under ambient conditions. The enzymes depend on the recently discovered prenylated FMN cofactor for catalysis, which is proposed to proceed via a monocovalently bound quinoid–cofactor intermediate.
ISSN:1433-7851
1521-3773
1521-3773
DOI:10.1002/anie.201708091