ArticleNature communications2022
Single amino acid bionanozyme for environmental remediation.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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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.
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Who cites it
32 citing papers in PubMed.
- Functional abiotic metabolite assembly hypothesis for the early events in the origin of life.Nature communications · 2026Review
- Integration of Laccase-like Nanozymes and Sensing Strategies for Food Quality and Safety Monitoring.Foods (Basel, Switzerland) · 2026Review
- Conserved catalytic motifs encode enzyme-like supramolecular peptide assemblies.Research square · 2026Article
- Recyclable Green Synthesis of CuAngewandte Chemie (International ed. in English) · 2026Article
- Nanozymes in Point-of-Care Testing: Classification, Biosensing Strategies, and Integrated Applications.Chemical record (New York, N.Y.) · 2026Review
- Glycine-Copper Nanozyme with Dual Oxidase Activity: for Colorimetric Detection of Epinephrine and Oxidation of Phenolic Pollutants.ACS omega · 2026Article
- Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Nanozymes for Energy and Environmental Sustainability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Regulating Promiscuous Catalysis via Substrate-Induced Transient Assembly.Angewandte Chemie (International ed. in English) · 2026Article
- Article
- Bioinspired Design of Heterogenous Single-Atomic-Site Catalysts for Electrocatalysis and Photocatalysis.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Thermophilic MoNCommunications chemistry · 2025Article
- A bioinformatics approach to design minimal biomimetic metal-binding peptides.Communications chemistry · 2025Article
- Multienzyme (3-in-1)-Mimicking a Single Nucleobase-Derived Bionanozyme for Versatile Environmental and Biomedical Applications.Advanced healthcare materials · 2025Article
- Mimic metalloenzymes with atomically dispersed Fe sites in covalent organic framework membranes for enhanced COChemical science · 2025Article
- Amino acid modified copper-based metal organic polyhedral with higher peroxidase activity for potassium guaiacol sulfonate detection.Scientific reports · 2025Article
- Precision Thermostability Predictions: Leveraging Machine Learning for Examining Laccases and Their Associated Genes.International journal of molecular sciences · 2024Article
- Copper formate-lysine nanoparticles with polyphenol oxidase-like activity for the detection of epinephrine.Analytical and bioanalytical chemistry · 2024Article
- Emerging chiral two-dimensional materials.Nature chemistry · 2024Review
- Unveiling the role of inorganic nanoparticles in Earth's biochemical evolution through electron transfer dynamics.iScience · 2024Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes are extremely complex catalytic structures with immense biological and technological importance. Nevertheless, their widespread environmental implementation faces several challenges, including high production costs, low operational stability, and intricate recovery and reusability. Therefore, the de novo design of minimalistic biomolecular nanomaterials that can efficiently mimic the biocatalytic function (bionanozymes) and overcome the limitations of natural enzymes is a critical goal in biomolecular engineering. Here, we report an exceptionally simple yet highly active and robust single amino acid bionanozyme that can catalyze the rapid oxidation of environmentally toxic phenolic contaminates and serves as an ultrasensitive tool to detect biologically important neurotransmitters similar to the laccase enzyme. While inspired by the laccase catalytic site, the substantially simpler copper-coordinated bionanozyme is ∼5400 times more cost-effective, four orders more efficient, and 36 times more sensitive compared to the natural protein. Furthermore, the designed mimic is stable under extreme conditions (pH, ionic strength, temperature, storage time), markedly reusable for several cycles, and displays broad substrate specificity. These findings hold great promise in developing efficient bionanozymes for analytical chemistry, environmental protection, and biotechnology.
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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.