Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 44, Pages 13893-13897Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201708091
Keywords
biocatalysis; carboxylation; catechols; prenylated FMN
Categories
Funding
- Austrian EWE [26863-N19]
- Austrian BMWFJ
- BMVIT
- SFG
- Standortagentur Tirol
- ZIT through the Austrian FFG-COMET Funding Program
- BBSRC grant [BB/K017802/1]
- BBSRC iCASE studentship
- Royal Society Wolfson Merit Award
- University of Graz
- Biotechnology and Biological Sciences Research Council [1352655, BB/K017802/1, BB/P000622/1] Funding Source: researchfish
- Austrian Science Fund (FWF) [P26863] Funding Source: Austrian Science Fund (FWF)
- BBSRC [BB/P000622/1, BB/K017802/1] Funding Source: UKRI
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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.
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