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Regioselective para-Carboxylation of Catechols by a Prenylated Flavin Dependent Decarboxylase

DOI: 10.1002/anie.201708091 DOI Help

Authors: Stefan Payer (University of Graz) , Stephen A. Marshall (University of Manchester) , Natalie Bärland (Max Planck Institute of Biophysics) , Xiang Sheng (Stockholm University) , Tamara Reiter (Austrian Centre of Industrial Biotechnology (ACIB)) , Andela Dordic (Austrian Centre of Industrial Biotechnology (ACIB)) , Georg Steinkellner (Austrian Centre of Industrial Biotechnology (ACIB)) , Christiane Wuensch (Austrian Centre of Industrial Biotechnology (ACIB)) , Susann Kaltwasser (Max Planck Institute of Biophysics) , Karl Fisher (Manchester Institute of Biotechnology, University of Manchester) , Stephen E. J. Rigby (Manchester Institute of Biotechnology, University of Manchester) , Peter Macheroux (Institute of Biochemistry, Graz University of Technology) , Janet Vonck (Max Planck Institute of Biophysics) , Karl Gruber (Institute of Molecular Biosciences, University of Graz) , Kurt Faber (University of Graz) , Fahmi Himo (Stockholm University) , David Leys (University of Manchester) , Tea Pavkov-keller (Institute of Molecular Biosciences, University of Graz) , Silvia M. Glueck (University of Graz)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie International Edition

State: Published (Approved)
Published: August 2017
Diamond Proposal Number(s): 12788

Abstract: The utilization of CO2 as carbon source for organic syntheses meets the urgent demand of more sustainability in chemical production. Here 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 confirm 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 a monocovalent quinoid-cofactor intermediate is proposed, which is distinct from the prFMN associated 1,3 dipolar cycloaddition mechanism in related enzymes.

Journal Keywords: Biocatalysis; Carboxylation; Catechols; prenylated; FMN

Subject Areas: Chemistry

Instruments: I03-Macromolecular Crystallography