ArticleNature communications2023
A supramolecular metalloenzyme possessing robust oxidase-mimetic catalytic function.
Article in Nature communications, 2023. 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, 45 citations in OpenAlex.
- Integration of Laccase-like Nanozymes and Sensing Strategies for Food Quality and Safety Monitoring.Foods (Basel, Switzerland) · 2026Review
- IrMn-Cluster-Based Artificial Metalloenzymes with Radiosensitized Systemic Antitumor Responses to Prevent Malignant Tumor Metastasis and Recurrence.Nano-micro letters · 2026Article
- Article
- Spatial Coordination Structure-Driven Enzyme-Like Selectivity in Single-Atom Nanozymes.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Bioinspired ruthenium-manganese-oxygen complex for biocatalytic and radiosensitization therapies to eradicate primary and metastatic tumors.Nature communications · 2025Article
- Article
- Peptide nanozymes: An emerging direction for functional enzyme mimics.Bioactive materials · 2024Review
- Copper formate-lysine nanoparticles with polyphenol oxidase-like activity for the detection of epinephrine.Analytical and bioanalytical chemistry · 2024Article
- Halogenated-edge polymeric semiconductor for efficient spin transport.Nature communications · 2024Article
- Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes fold into unique three-dimensional structures to distribute their reactive amino acid residues, but environmental changes can disrupt their essential folding and lead to irreversible activity loss. The de novo synthesis of enzyme-like active sites is challenging due to the difficulty of replicating the spatial arrangement of functional groups. Here, we present a supramolecular mimetic enzyme formed by self-assembling nucleotides with fluorenylmethyloxycarbonyl (Fmoc)-modified amino acids and copper. This catalyst exhibits catalytic functions akin those of copper cluster-dependent oxidases, and catalytic performance surpasses to date-reported artificial complexes. Our experimental and theoretical results reveal the crucial role of periodic arrangement of amino acid components, enabled by fluorenyl stacking, in forming oxidase-mimetic copper clusters. Nucleotides provide coordination atoms that enhance copper activity by facilitating the formation of a copper-peroxide intermediate. The catalyst shows thermophilic behavior, remaining active up to 95 °C in an aqueous environment. These findings may aid the design of advanced biomimetic catalysts and offer insights into primordial redox enzymes.
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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.