ArticleJournal of the American Chemical Society2011
Controlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.
Article in Journal of the American Chemical Society, 2011. 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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22 citing papers in PubMed, 39 citations in OpenAlex.
- Photocatalytic Hydrogen Evolution by a De Novo Designed Metalloprotein that Undergoes Ni-Mediated Oligomerization Shift.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Review
- How Outer Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Catalytic peptide assemblies.Chemical Society reviews · 2018Review
- Gating of Connexin Channels by transjunctional-voltage: Conformations and models of open and closed states.Biochimica et biophysica acta. Biomembranes · 2018Review
- Incorporation of second coordination sphere D-amino acids alters Cd(II) geometries in designed thiolate-rich proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Lead(II) Binding in Natural and Artificial Proteins.Metal ions in life sciences · 2017Article
- Direct Observation of Nanosecond Water Exchange Dynamics at a Protein Metal Site.Journal of the American Chemical Society · 2017Article
- Location dependent coordination chemistry and MRI relaxivity, inChemical science · 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
- Variable primary coordination environments of Cd(II) binding to three helix bundles provide a pathway for rapid metal exchange.Metallomics : integrated biometal science · 2015Article
- De novo protein design as a methodology for synthetic bioinorganic chemistry.Accounts of chemical research · 2015Article
- Metal coordination study at Ag and Cd sites in crown thioether complexes through DFT calculations and hyperfine parameters.Journal of molecular modeling · 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
- Designing functional metalloproteins: from structural to catalytic metal sites.Coordination chemistry reviews · 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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4 authors at 3 institutions in 3 countries.
Funding
Abstract
Herein we report how de novo designed peptides can be used to investigate whether the position of a metal site along a linear sequence that folds into a three-stranded α-helical coiled coil defines the physical properties of Cd(II) ions in either CdS(3) or CdS(3)O (O-being an exogenous water molecule) coordination environments. Peptides are presented that bind Cd(II) into two identical coordination sites that are located at different topological positions at the interior of these constructs. The peptide GRANDL16PenL19IL23PenL26I binds two Cd(II) as trigonal planar 3-coordinate CdS(3) structures whereas GRANDL12AL16CL26AL30C sequesters two Cd(II) as pseudotetrahedral 4-coordinate CdS(3)O structures. We demonstrate how for the first peptide, having a more rigid structure, the location of the identical binding sites along the linear sequence does not affect the physical properties of the two bound Cd(II). However, the sites are not completely independent as Cd(II) bound to one of the sites ((113)Cd NMR chemical shift of 681 ppm) is perturbed by the metalation state (apo or [Cd(pep)(Hpep)(2)](+) or [Cd(pep)(3)](-)) of the second center ((113)Cd NMR chemical shift of 686 ppm). GRANDL12AL16CL26AL30C shows a completely different behavior. The physical properties of the two bound Cd(II) ions indeed depend on the position of the metal center, having pK(a2) values for the equilibrium [Cd(pep)(Hpep)(2)](+) → [Cd(pep)(3)](-) + 2H(+) (corresponding to deprotonation and coordination of cysteine thiols) that range from 9.9 to 13.9. In addition, the L26AL30C site shows dynamic behavior, which is not observed for the L12AL16C site. These results indicate that for these systems one cannot simply assign a "4-coordinate structure" and assume certain physical properties for that site since important factors such as packing of the adjacent Leu, size of the intended cavity (endo vs exo) and location of the metal site play crucial roles in determining the final properties of the bound Cd(II).
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