ArticleInorganic chemistry2015
De novo design and characterization of copper metallopeptides inspired by native cupredoxins.
Article in 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.
- Azurins With Tunable Reduction Potentials as Redox Mediators for Extracellular Electron Transfer.Chembiochem : a European journal of chemical biology · 2026Article
- Probing anion recognition in a cobalt(II) de novo designed metalloprotein.Journal of inorganic biochemistry · 2026Article
- Structural insights into copper and zinc binding to tau protein and the impact of metal binding on amyloid aggregation.Chemical science · 2026Article
- A De Novo Designed Metalloprotein Displays Variable Thermal Stability and Binding Stoichiometry with Transition Metal Ions.Chembiochem : a European journal of chemical biology · 2025Article
- Exploring the influence of H-bonding and ligand constraints on thiolate ligated non-heme iron mediated dioxygen activation.Chemical science · 2024Article
- 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
- De Novo Design of a Self-Assembled Artificial Copper Peptide that Activates and Reduces Peroxide.ACS catalysis · 2021Article
- A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases.Molecules (Basel, Switzerland) · 2021Review
- Traversing the Red-Green-Blue Color Spectrum in Rationally Designed Cupredoxins.Journal of the American Chemical Society · 2020Article
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- Rational De Novo Design of a Cu Metalloenzyme for Superoxide Dismutation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Selective coordination of three transition metal ions within a coiled-coil peptide scaffold.Chemical science · 2019Article
- Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.Inorganic chemistry · 2018Article
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- Development of a Rubredoxin-Type Center Embedded in a de Dovo-Designed Three-Helix Bundle.Biochemistry · 2018Article
- Modular Artificial Cupredoxins.Journal of the American Chemical Society · 2016Article
- Electron transfer activity of a de novo designed copper center in a three-helix bundle fold.Biochimica et biophysica acta · 2016Article
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7 authors.
Funding
Abstract
Using de novo protein design, we incorporated a copper metal binding site within the three-helix bundle α3D (Walsh et al. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 5486-5491) to assess whether a cupredoxin center within an α-helical domain could mimic the spectroscopic, structural, and redox features of native type-1 copper (CuT1) proteins. We aimed to determine whether a CuT1 center could be realized in a markedly different scaffold rather than the native β-barrel fold and whether the characteristic short Cu-S bond (2.1-2.2 Å) and positive reduction potentials could be decoupled from the spectroscopic properties (ε600 nm = 5000 M(-1) cm(-1)) of such centers. We incorporated 2HisCys(Met) residues in three distinct α3D designs designated core (CR), chelate (CH), and chelate-core (ChC). XAS analysis revealed a coordination environment similar to reduced CuT1 proteins, producing Cu-S(Cys) bonds ranging from 2.16 to 2.23 Å and Cu-N(His) bond distances of 1.92-1.99 Å. However, Cu(II) binding to the CR and CH constructs resulted in tetragonal type-2 copper-like species, displaying an intense absorption band between 380 and 400 nm (>1500 M(-1) cm(-1)) and A|| values of (150-185) × 10(-4) cm(-4). The ChC construct, which possesses a metal-binding site deeper in its helical bundle, yielded a CuT1-like brown copper species, with two absorption bands at 401 (4429 M(-1) cm(-1)) and 499 (2020 M(-1) cm(-1)) nm and an A|| value ∼30 × 10(-4) cm(-4) greater than its native counterparts. Electrochemical studies demonstrated reduction potentials of +360 to +460 mV (vs NHE), which are within the observed range for azurin and plastocyanin. These observations showed that the designed metal binding sites lacked the necessary rigidity to enforce the appropriate structural constraints for a Cu(II) chromophore (EPR and UV-vis); however, the Cu(I) structural environment and the high positive potential of CuT1 centers were recapitulated within the α-helical bundle of α3D.
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