Vanadium-dependent haloperoxidases from diverse microbes halogenate exogenous alkyl quinolone quorum sensing signals DOI Creative Commons
Jackson T. Baumgartner, Catherine S. McCaughey,

Hanna S. Fleming

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Aug. 1, 2024

Site-selective vanadium-dependent haloperoxidases (VHPOs) are a unique enzyme family that catalyze selective halogenation reactions previously characterized within bacterial natural product biosynthetic pathways. However, the broader chemical roles and biological distribution of these halogenases remains to be explored. Using bioinformatic methods, we have defined VHPO subfamily regioselectively brominates alkyl quinolone (AQ) quorum sensing molecules.

Language: Английский

Intermolecular 1,2,4-Thiadiazole Synthesis Enabled by Enzymatic Halide Recycling with Vanadium-Dependent Haloperoxidases DOI Creative Commons
Manik Sharma, Cameron A. Pascoe, Stacey K. Jones

et al.

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: March 12, 2025

The enzymatic synthesis of heterocycles is an emerging biotechnology for the sustainable construction societally important molecules. Herein, we describe enzyme-mediated strategy oxidative dimerization thioamides enabled by halide recycling vanadium-dependent haloperoxidase enzymes. This approach allows intermolecular biocatalytic bond formation using a catalytic quantity salt and hydrogen peroxide as terminal oxidant. established method applied to diverse range generate corresponding 1,2,4-thiadiazoles in moderate high yields with excellent chemoselectivity. Mechanistic experiments suggest that reaction proceeds through two distinct sulfur halogenation events are critical heterocycle formation. Molecular docking provide insight into reactivity differences between biocatalysts used this study. Finally, developed preparative scale chemoenzymatic anticancer agent penicilliumthiamine B. These studies demonstrate promising platform

Language: Английский

Citations

2
Regioselective Halogenation of Lavanducyanin by a Site-Selective Vanadium-Dependent Chloroperoxidase DOI Creative Commons
Jackson T. Baumgartner, Shaun M. K. McKinnie

Organic Letters, Journal Year: 2024, Volume and Issue: 26(27), P. 5725 - 5730

Published: June 27, 2024

Halogenated phenazine meroterpenoids are a structurally unusual family of marine actinobacterial natural products that exhibit antibiotic, antibiofilm, and cytotoxic bioactivities. Despite lack established halogenation biochemistry, genomic analysis

Language: Английский

Citations

5
Biocatalytic Thioketal Cleavage Enabled by Enzymatic Bromide Recycling by Vanadium-Dependent Haloperoxidases DOI Creative Commons
Manik Sharma, Ying Li, Kyle F. Biegasiewicz

et al.

Organic Letters, Journal Year: 2025, Volume and Issue: unknown

Published: May 20, 2025

Thioketalsa are an important class of molecules used for the preparation and protection carbonyl compounds in chemical synthesis. Selective cleavage thioketals requires use harsh conditions reagents that limit chemoenzymatic Herein, we describe a biocatalytic strategy using enzymatic bromide recycling by vanadium-dependent haloperoxidase (VHPO) enzymes. This reaction design involves halogenation-mediated thioketal through repetitive enzyme-mediated formation hypobromous acid with catalytic quantity salt hydrogen peroxide as terminal oxidant. protocol is demonstrated on broad range 1,3-dithiolanes high yield excellent chemoselectivity, performed gram scale, run lysate whole cells, applied to 1,3-dithianes 1,3-oxathiolanes.

Language: Английский

Citations

0
Chemoenzymatic C,C-Bond Forming Cascades by Cryptic Vanadium Haloperoxidase Catalyzed Bromination DOI Creative Commons

Qingqi Zhao,

Ru Zhang, Johannes Döbber

et al.

Organic Letters, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 31, 2024

Inspired by natural cryptic halogenation in C,C-bond formation, this study developed a synthetic approach combining biocatalytic bromination with transition-metal-catalyzed cross-coupling. Using the cyanobacterial AmVHPO, robust and sustainable bromination-arylation cascade was created. Genetic modifications allowed enzyme immobilization, enhancing compatibility between biocatalysis chemocatalysis. This mild, efficient method for synthesizing biaryl compounds provides foundation future biochemo reactions harnessing as traceless directing tool.

Language: Английский

Citations

3
Vanadium-dependent haloperoxidases from diverse microbes halogenate exogenous alkyl quinolone quorum sensing signals DOI Creative Commons
Jackson T. Baumgartner, Catherine S. McCaughey,

Hanna S. Fleming

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Aug. 1, 2024

Site-selective vanadium-dependent haloperoxidases (VHPOs) are a unique enzyme family that catalyze selective halogenation reactions previously characterized within bacterial natural product biosynthetic pathways. However, the broader chemical roles and biological distribution of these halogenases remains to be explored. Using bioinformatic methods, we have defined VHPO subfamily regioselectively brominates alkyl quinolone (AQ) quorum sensing molecules.

Language: Английский

Citations

1