ArticleACS central science2021
A Dual Anchoring Strategy for the Directed Evolution of Improved Artificial Transfer Hydrogenases Based on Carbonic Anhydrase.
Article in ACS central science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Artificial metalloenzymes in complex biological environments.Nature chemical biology · 2026Review
- Article
- Catalyzed Enantioselective Organic Synthesis.ACS central science · 2025Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
- Generating Site Saturation Mutagenesis Libraries and Transferring Them to Broad Host-Range Plasmids Using Golden Gate Cloning.Methods in molecular biology (Clifton, N.J.) · 2025Article
- De novo design and evolution of an artificial metathase for cytoplasmic olefin metathesis.Nature catalysis · 2025Article
- Understanding Structural Isomerism in Organoiridium Picolinamidate Complexes and its Consequences on Reactivity and Biological Properties.Inorganic chemistry frontiers · 2024Article
- Ru(ii)/Os(ii)-based carbonic anhydrase inhibitors as photodynamic therapy photosensitizers for the treatment of hypoxic tumours.Chemical science · 2023Article
- First and second sphere interactions accelerate non-nativeChemical communications (Cambridge, England) · 2023Article
- Dynamic Ir(III) Photosensors for the Major Human Drug-Metabolizing Enzyme Cytochrome P450 3A4.Inorganic chemistry · 2023Article
- Mechanistic and structural characterization of an iridium-containing cytochrome reveals kinetically relevant cofactor dynamics.Nature catalysis · 2023Article
- Ir(III)-Based Agents for Monitoring the Cytochrome P450 3A4 Active Site Occupancy.Inorganic chemistry · 2022Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Artificial metalloenzymes result from anchoring a metal cofactor within a host protein. Such hybrid catalysts combine the selectivity and specificity of enzymes with the versatility of (abiotic) transition metals to catalyze new-to-nature reactions in an evolvable scaffold. With the aim of improving the localization of an arylsulfonamide-bearing iridium-pianostool catalyst within human carbonic anhydrase II (hCAII) for the enantioselective reduction of prochiral imines, we introduced a covalent linkage between the host and the guest. Herein, we show that a judiciously positioned cysteine residue reacts with a
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Registered trials
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