ArticleProceedings of the National Academy of Sciences of the United States of America2012
Designing a functional type 2 copper center that has nitrite reductase activity within α-helical coiled coils.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Probing anion recognition in a cobalt(II) de novo designed metalloprotein.Journal of inorganic biochemistry · 2026Article
- When the wrong metal stops the cycle: Dynamics and specificity in plant copper-dependent peptide cyclases.Journal of inorganic biochemistry · 2026Article
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
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- A bioinformatics approach to design minimal biomimetic metal-binding peptides.Communications chemistry · 2025Article
- Mechanism of Oxidative C─H Bond Activation by De Novo Designed Artificial Cu Metalloenzymes Using HChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Recent advances in de novo designed metallopeptides as tailored enzyme mimics.Current opinion in chemical biology · 2025Review
- Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes.Nature communications · 2025Article
- Molecular Origami: Designing Functional Molecules of the Future.Molecules (Basel, Switzerland) · 2025Review
- Nitrite Reductases in Biomedicine: From Natural Enzymes to Artificial Mimics.Research (Washington, D.C.) · 2025Review
- Breaking symmetry: Metal-guided assembly of heterotrimeric coiled coils.Methods in enzymology · 2025Article
- Revving up a Designed Copper Nitrite Reductase Using Non-Coded Active Site Ligands.ACS catalysis · 2024Article
- Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries.Journal of the American Chemical Society · 2023Article
- Design of the elusive proteinaceous oxygen donor copper site suggests a promising future for copper for MRI contrast agents.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- YfeX - A New Platform for Carbene Transferase Development with High Intrinsic Reactivity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Nitrite reductase activity within an antiparallel de novo scaffold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
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5 authors.
Funding
Abstract
One of the ultimate objectives of de novo protein design is to realize systems capable of catalyzing redox reactions on substrates. This goal is challenging as redox-active proteins require design considerations for both the reduced and oxidized states of the protein. In this paper, we describe the spectroscopic characterization and catalytic activity of a de novo designed metallopeptide Cu(I/II)(TRIL23H)(3)(+/2+), where Cu(I/II) is embeded in α-helical coiled coils, as a model for the Cu(T2) center of copper nitrite reductase. In Cu(I/II)(TRIL23H)(3)(+/2+), Cu(I) is coordinated to three histidines, as indicated by X-ray absorption data, and Cu(II) to three histidines and one or two water molecules. Both ions are bound in the interior of the three-stranded coiled coils with affinities that range from nano- to micromolar [Cu(II)], and picomolar [Cu(I)]. The Cu(His)(3) active site is characterized in both oxidation states, revealing similarities to the Cu(T2) site in the natural enzyme. The species Cu(II)(TRIL23H)(3)(2+) in aqueous solution can be reduced to Cu(I)(TRIL23H)(3)(+) using ascorbate, and reoxidized by nitrite with production of nitric oxide. At pH 5.8, with an excess of both the reductant (ascorbate) and the substrate (nitrite), the copper peptide Cu(II)(TRIL23H)(3)(2+) acts as a catalyst for the reduction of nitrite with at least five turnovers and no loss of catalytic efficiency after 3.7 h. The catalytic activity, which is first order in the concentration of the peptide, also shows a pH dependence that is described and discussed.
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