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

Stefan E Payer; Stephen A Marshall; Natalie Bärland; Xiang Sheng; Tamara Reiter; Andela Dordic; Georg Steinkellner; Christiane Wuensch; Susann Kaltwasser; Karl Fisher; Stephen E J Rigby; Peter Macheroux; Janet Vonck; Karl Gruber; Kurt Faber; Fahmi Himo; David Leys; Tea Pavkov-Keller; Silvia M Glueck

doi:10.1002/anie.201708091

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

Angew Chem Int Ed Engl. 2017 Oct 23;56(44):13893-13897. doi: 10.1002/anie.201708091. Epub 2017 Oct 2.

Authors

Stefan E Payer¹, Stephen A Marshall², Natalie Bärland³, Xiang Sheng⁴, Tamara Reiter⁵, Andela Dordic^{6

5}, Georg Steinkellner^{6

5}, Christiane Wuensch⁵, Susann Kaltwasser³, Karl Fisher², Stephen E J Rigby², Peter Macheroux⁷, Janet Vonck³, Karl Gruber⁶, Kurt Faber¹, Fahmi Himo⁴, David Leys², Tea Pavkov-Keller^{6

5}, Silvia M Glueck^{1

5}

Affiliations

¹ Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, NAWI Graz, BioTechMed Graz, Heinrichstrasse 28/2, 8010, Graz, Austria.
² Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
³ Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, 60438, Frankfurt am Main, Germany.
⁴ Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, 10691, Stockholm, Sweden.
⁵ Austrian Centre of Industrial Biotechnology (ACIB), Austria.
⁶ Institute of Molecular Biosciences, University of Graz, NAWI Graz, BioTechMed Graz, Humboldtstrasse 50, 8010, Graz, Austria.
⁷ Institute of Biochemistry, Graz University of Technology, Petersgasse 12, 8010, Graz, Austria.

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.

Keywords: biocatalysis; carboxylation; catechols; prenylated FMN.

Publication types

Research Support, Non-U.S. Gov't

Abstract

Publication types

Grants and funding