ReviewMolecules (Basel, Switzerland)2019
Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters.
Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Programming Mn(II) coordination in self-assembling peptides amplifies mtDNA-driven STING signaling for potent antitumor immunity.Materials today. Bio · 2026Article
- Comparative Analysis of Hulless Barley Transcriptomes to Regulatory Effects of Phosphorous Deficiency.Life (Basel, Switzerland) · 2024Article
- Dye Decolorization by a Miniaturized Peroxidase Fe-MimochromeVI*a.International journal of molecular sciences · 2023Article
- Exploring the Reactivity of Polyoxometalates toward Proteins: From Interactions to Mechanistic Insights.JACS Au · 2023Review
- Pyrrolyl and Indolyl α-γ-Diketo Acid Derivatives Acting as Selective Inhibitors of Human Carbonic Anhydrases IX and XII.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Changing the tracks: screening for electron transfer proteins to support hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Molecular Dynamics Simulation and Kinetic Study of Fluoride Binding to V21C/V66C Myoglobin with a Cytoglobin-like Disulfide Bond.International journal of molecular sciences · 2020Article
- Uranyl Binding to Proteins and Structural-Functional Impacts.Biomolecules · 2020Review
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Authors and funding
1 author.
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Abstract
Metalloproteins and metalloenzymes play important roles in biological systems by using the limited metal ions, complexes, and clusters that are associated with the protein matrix. The design of artificial metalloproteins and metalloenzymes not only reveals the structure and function relationship of natural proteins, but also enables the synthesis of artificial proteins and enzymes with improved properties and functions. Acknowledging the progress in rational design from single to multiple active sites, this review focuses on recent achievements in the design of artificial metalloproteins and metalloenzymes with metal clusters, including zinc clusters, cadmium clusters, iron-sulfur clusters, and copper-sulfur clusters, as well as noble metal clusters and others. These metal clusters were designed in both native and de novo protein scaffolds for structural roles, electron transfer, or catalysis. Some synthetic metal clusters as functional models of native enzymes are also discussed. These achievements provide valuable insights for deep understanding of the natural proteins and enzymes, and practical clues for the further design of artificial enzymes with functions comparable or even beyond those of natural counterparts.
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Registered trials
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