ArticleEuropean journal of inorganic chemistry2015
Artificial Diiron Enzymes with a De Novo Designed Four-Helix Bundle Structure.
Article in European journal of inorganic chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- From duplication to fusion: Expanding Dayhoff's model of protein evolution.Protein science : a publication of the Protein Society · 2025Review
- Important Structural Features of Thiolate-Rich Four-Helix Bundles for Cu(I) Uptake and Removal.Inorganic chemistry · 2023Article
- Exploration of Structured Symmetric Cyclic Peptides as Ligands for Metal-Organic Frameworks.Chemistry of materials : a publication of the American Chemical Society · 2022Article
- A bound iron porphyrin is redox active in hybrid bacterial reaction centers modified to possess a four-helix bundle domain.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Rational design of photosynthetic reaction center protein maquettes.Frontiers in molecular biosciences · 2022Article
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Unravelling the Structure of the Tetrahedral Metal-Binding Site in METP3 through an Experimental and Computational Approach.Molecules (Basel, Switzerland) · 2021Article
- A de novo binuclear zinc enzyme with DNA cleavage activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Use of an Artificial Miniaturized Enzyme in Hydrogen Peroxide Detection by Chemiluminescence.Sensors (Basel, Switzerland) · 2020Article
- Enantioselective Hydroxylation of Benzylic C(spJournal of the American Chemical Society · 2020Article
- Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To Go.ACS catalysis · 2018Article
- Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster.Biopolymers · 2018Article
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- Rapid Sampling of Hydrogen Bond Networks for Computational Protein Design.Journal of chemical theory and computation · 2018Article
- De Novo Design of Tetranuclear Transition Metal Clusters Stabilized by Hydrogen-Bonded Networks in Helical Bundles.Journal of the American Chemical Society · 2018Article
- Computer-aided design of amino acid-based therapeutics: a review.Drug design, development and therapy · 2018Review
- Visualizing Biological Copper Storage: The Importance of Thiolate-Coordinated Tetranuclear Clusters.Angewandte Chemie (International ed. in English) · 2017Article
- The role of directional interactions in the designability of generalized heteropolymers.Scientific reports · 2017Article
- d-Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- Design and engineering of artificial oxygen-activating metalloenzymes.Chemical Society reviews · 2016Review
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Authors and funding
6 authors.
Funding
Abstract
A single polypeptide chain may provide an astronomical number of conformers. Nature selected only a trivial number of them through evolution, composing an alphabet of scaffolds, that can afford the complete set of chemical reactions needed to support life. These structural templates are so stable that they allow several mutations without disruption of the global folding, even having the ability to bind several exogenous cofactors. With this perspective, metal cofactors play a crucial role in the regulation and catalysis of several processes. Nature is able to modulate the chemistry of metals, adopting only a few ligands and slightly different geometries. Several scaffolds and metal-binding motifs are representing the focus of intense interest in the literature. This review discusses the widespread four-helix bundle fold, adopted as a scaffold for metal binding sites in the context of de novo protein design to obtain basic biochemical components for biosensing or catalysis. In particular, we describe the rational refinement of structure/function in diiron-oxo protein models from the
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