ArticleDalton transactions (Cambridge, England : 2003)2009
Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.
Article in Dalton transactions (Cambridge, England : 2003), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Revving up a Designed Copper Nitrite Reductase Using Non-Coded Active Site Ligands.ACS catalysis · 2024Article
- 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
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- How Outer Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Modifying the Steric Properties in the Second Coordination Sphere of Designed Peptides Leads to Enhancement of Nitrite Reductase Activity.Angewandte Chemie (International ed. in English) · 2018Article
- d-Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- Lead(II) Binding in Natural and Artificial Proteins.Metal ions in life sciences · 2017Article
- A Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed Metalloproteins.Journal of the American Chemical Society · 2016Article
- De Novo Design of Metalloproteins and Metalloenzymes in a Three-Helix Bundle.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Methods for Solving Highly Symmetric De Novo Designed Metalloproteins: Crystallographic Examination of a Novel Three-Stranded Coiled-Coil Structure Containing d-Amino Acids.Methods in enzymology · 2016Article
- Oxidation Protection in Metal-Binding Peptide Motif and Its Application to Antibody for Site-Selective Conjugation.PloS one · 2016Article
- Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy Metals.Biochemistry · 2015Article
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Sculpting Metal-binding Environments inIsrael journal of chemistry · 2015Article
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- De novo design of Ln(III) coiled coils for imaging applications.Journal of the American Chemical Society · 2014Article
- De novo-designed metallopeptides with type 2 copper centers: modulation of reduction potentials and nitrite reductase activities.Journal of the American Chemical Society · 2013Article
- Designing functional metalloproteins: from structural to catalytic metal sites.Coordination chemistry reviews · 2013Article
- Controlling self-assembly of a peptide-based material via metal-ion induced registry shift.Journal of the American Chemical Society · 2013Article
- Influence of active site location on catalytic activity in de novo-designed zinc metalloenzymes.Journal of the American Chemical Society · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
Advances in protein chemistry and molecular and structural biology have empowered modern chemists to build complex biological architectures using a "first principles" approach, which is known as de novo protein design. In this Perspective we demonstrate how simple three-stranded alpha-helical constructs can be prepared by the sole consideration of the primary amino acid sequence of a peptide. With these well defined systems, we then demonstrate that metal binding cavities can be carved out of the hydrophobic cores of these aggregates in order to bind metal ions such as cadmium with well defined coordination geometries. Examples will be given of homoleptic CdS(3) complexes, CdS(3)O sites and proteins which contain equilibrium mixtures of these two species. We will provide a description of a strategy that allows us to build heterochromic peptides (small proteins that complex two metals in nearly identical environments but which result in different physical properties and allow for metal site selectivity). We conclude with a new class of designed peptides, diastereopeptides, which can exploit changes in amino acid chirality to control metal ion coordination number and lead to an alternative path towards heterochromic systems. The constructs described herein represent the initial steps of preparing protein structures that may simultaneous contain structural and catalytic metal binding centers. These studies inform the community on a developing field, which promises new opportunities for the study of bioinorganic chemistry.
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