ArticleNature chemistry2024
An evolved artificial radical cyclase enables the construction of bicyclic terpenoid scaffolds via an H-atom transfer pathway.
Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- Artificial metalloenzymes in complex biological environments.Nature chemical biology · 2026Review
- A biocatalytic platform for the stereoselective synthesis of diverse atropisomeric compounds using engineered metalloenzymes.Science advances · 2026Article
- Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026Article
- Enantioselective electrophilic α-fluorination catalyzed by an artificial metalloenzyme.Chemical science · 2026Article
- Enzymatic Metal-Hydrogen Atom Transfer with a Cobalt Protoporphyrin Cofactor.Journal of the American Chemical Society · 2026Article
- 50 Years of Giese Reaction - a Personal View.Angewandte Chemie (International ed. in English) · 2026Review
- Article
- A cytokine-based designer enzyme with an abiological multinuclear metal center exhibits intrinsic and extrinsic catalysis.Nature communications · 2025Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
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Authors and funding
12 authors.
Funding
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Abstract
While natural terpenoid cyclases generate complex terpenoid structures via cationic mechanisms, alternative radical cyclization pathways are underexplored. The metal-catalysed H-atom transfer reaction (M-HAT) offers an attractive means for hydrofunctionalizing olefins, providing access to terpenoid-like structures. Artificial metalloenzymes offer a promising strategy for introducing M-HAT reactivity into a protein scaffold. Here we report our efforts towards engineering an artificial radical cyclase (ARCase), resulting from anchoring a biotinylated [Co(Schiff-base)] cofactor within an engineered chimeric streptavidin. After two rounds of directed evolution, a double mutant catalyses a radical cyclization to afford bicyclic products with a cis-5-6-fused ring structure and up to 97% enantiomeric excess. The involvement of a histidine ligation to the Co cofactor is confirmed by crystallography. A time course experiment reveals a cascade reaction catalysed by the ARCase, combining a radical cyclization with a conjugate reduction. The ARCase exhibits tolerance towards variations in the dienone substrate, highlighting its potential to access terpenoid scaffolds.
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