ArticleScience (New York, N.Y.)2016
An artificial metalloenzyme with the kinetics of native enzymes.
Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
105 citing papers in PubMed, 370 citations in OpenAlex.
- Photometallobiocatalytic Asymmetric Radical-Mediated Cross-Coupling of Organotrifluoroborate Salts and Pyridotriazoles.Angewandte Chemie (International ed. in English) · 2026Article
- Engineering an Artificial Metalloenzyme for Efficient Photo-Enzymatic COAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026Article
- Tailoring vanadium-doped carbon dots as a peroxidase mimic for precise colorimetric sensing of myricetin.Mikrochimica acta · 2026Article
- Directed evolution of enzymes at the crossroads of tradition and innovation.FEBS open bio · 2026Review
- Enzymatic Metal-Hydrogen Atom Transfer with a Cobalt Protoporphyrin Cofactor.Journal of the American Chemical Society · 2026Article
- High-Throughput Screening of Co-Protoporphyrin IX-Binding Proteins for Enhanced Hydrogen Production.Molecules (Basel, Switzerland) · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Biocatalytic kinetic resolution for efficient and enantioselective synthesis of δ-haloalcohols and tetrahydrofurans.Communications chemistry · 2025Article
- Porphyrins as cofactors in enzyme-catalyzed organic reactions.Biophysics reports · 2025Article
- Expanding the Terpene Universe: Synthetic Biology and Non-Natural Chemistry in Engineered Microorganisms.Molecules (Basel, Switzerland) · 2025Review
- In Situ Valence Engineering of Copper Silicate Nanozymes with Enhanced Peroxidase-Like Catalytic Activity for Oral Disease Detection.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
- Ligand-controlled divergent asymmetric C(spNature communications · 2025Article
- Iridium porphyrin-catalysed asymmetric carbene insertion into primary N-adjacent C-H bonds with TON over 1000000.Nature communications · 2025Article
- De novo design and evolution of an artificial metathase for cytoplasmic olefin metathesis.Nature catalysis · 2025Article
- Bimetallic clusterzymes-loaded dendritic mesoporous silica particle regulate arthritis microenvironmentBioactive materials · 2024Article
- Radical-Mediated Regiodivergent C(Chem catalysis · 2024Article
- Hybrid Metal Catalysts as Valuable Tools in Organic Synthesis: An Overview of the Recent Advances in Asymmetric C─C Bond Formation Reactions.Molecules (Basel, Switzerland) · 2024Review
- Microbial Mineralization withEnvironmental science & technology · 2024Article
45 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Natural enzymes contain highly evolved active sites that lead to fast rates and high selectivities. Although artificial metalloenzymes have been developed that catalyze abiological transformations with high stereoselectivity, the activities of these artificial enzymes are much lower than those of natural enzymes. Here, we report a reconstituted artificial metalloenzyme containing an iridium porphyrin that exhibits kinetic parameters similar to those of natural enzymes. In particular, variants of the P450 enzyme CYP119 containing iridium in place of iron catalyze insertions of carbenes into C-H bonds with up to 98% enantiomeric excess, 35,000 turnovers, and 2550 hours
Indexed as
Identifiers
What OpenQuestion holds
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.