Regioselective para‐Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase. Issue 44 (2nd October 2017)

• Record Type: Journal Article
• 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.
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 44(2017)
• Page Start: 13893
• Page End: 13897
• Publication Date: 2017-10-02
• Subjects: biocatalysis -- carboxylation -- catechols -- prenylated FMN; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201708091
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: 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 prFMN iminium 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. Abstract : 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.