ArticleACS catalysis2021
Engineering a Metathesis-Catalyzing Artificial Metalloenzyme Based on HaloTag.
Article in ACS catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Bioorthogonal Gold-Catalyzed Hydrothiolation Leading to Amide Bond Cleavage of Ethynylated Biarylbutanamide Precursors.Journal of the American Chemical Society · 2026Article
- Article
- Artificial Metalloenzymes in Artificial Sanctuaries Through Liquid-Liquid Phase Separation.Bio-protocol · 2025Article
- Artificial metalloenzyme assembly in cellular compartments for enhanced catalysis.Nature chemical biology · 2025Article
- BenzoHTag, a fluorogenic self-labeling protein developed using molecular evolution.bioRxiv : the preprint server for biology · 2024Article
- Catalytic olefin metathesis in blood.Chemical science · 2023Article
- Water-Accelerated Decomposition of Olefin Metathesis Catalysts.ACS catalysis · 2023Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Reactivity of Myoglobin Reconstituted with Cobalt Corrole toward Hydrogen Peroxide.International journal of molecular sciences · 2022Article
- Inside a Shell-Organometallic Catalysis Inside Encapsulin Nanoreactors.Angewandte Chemie (International ed. in English) · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Artificial metalloenzymes (ArMs) are created by embedding a synthetic metal catalyst into a protein scaffold. ArMs have the potential to merge the catalytic advantages of natural enzymes with the reaction scope of synthetic catalysts. The choice of the protein scaffold is of utmost importance to tune the activity of the ArM. Herein, we show the repurposing of HaloTag, a self-labeling protein widely used in chemical biology, to create an ArM scaffold for metathesis. This monomeric protein scaffold allows for covalent attachment of metathesis cofactors, and the resulting ArMs are capable of catalyzing ring-closing metathesis. Both chemical and genetic engineering were explored to determine the evolvability of the resulting ArM. Additionally, exploration of the substrate scope revealed a reaction with promising turnover numbers (>48) and conversion rates (>96%).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.