ArticleProceedings of the National Academy of Sciences of the United States of America2003
Hg(II) binding to a weakly associated coiled coil nucleates an encoded metalloprotein fold: a kinetic analysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 55 citations in OpenAlex.
- A De Novo Designed Metalloprotein Displays Variable Thermal Stability and Binding Stoichiometry with Transition Metal Ions.Chembiochem : a European journal of chemical biology · 2025Article
- Heteromeric three-stranded coiled coils designed using a Pb(II)(Cys)Nature chemistry · 2020Article
- How Outer Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- 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
- Preface.Methods in enzymology · 2016Article
- Sculpting Metal-binding Environments inIsrael journal of chemistry · 2015Article
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Designing hydrolytic zinc metalloenzymes.Biochemistry · 2014Review
- Designing functional metalloproteins: from structural to catalytic metal sites.Coordination chemistry reviews · 2013Article
- Probing the coordination environment of the human copper chaperone HAH1: characterization of Hg(II)-bridged homodimeric species in solution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2013Article
- Controlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.Journal of the American Chemical Society · 2011Article
- Ca 2+-induced self-assembly in designed peptides with optimally spaced gamma-carboxyglutamic acid residues.Journal of inorganic biochemistry · 2011Article
- Probing a homoleptic PbS3 coordination environment in a designed peptide using 207Pb NMR spectroscopy: implications for understanding the molecular basis of lead toxicity.Angewandte Chemie (International ed. in English) · 2010Article
- Structural comparisons of apo- and metalated three-stranded coiled coils clarify metal binding determinants in thiolate containing designed peptides.Journal of the American Chemical Society · 2010Article
- Design of functional metalloproteins.Nature · 2009Review
- Characterization of the cofactor-induced folding mechanism of a zinc-binding peptide using computationally designed mutants.Journal of molecular biology · 2009Article
- Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.Dalton transactions (Cambridge, England : 2003) · 2009Article
- Metal-binding dependent disruption of membranes by designed helices.Journal of the American Chemical Society · 2009Article
- Design of thiolate rich metal binding sites within a peptidic framework.Inorganic chemistry · 2008Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A detailed kinetic analysis of metal encapsulation by a de novo-designed protein is described. The kinetic mechanism of Hg(II) encapsulation in the three-stranded coiled coil formed by the peptide CH(3)CO-G LKALEEK CKALEEK LKALEEK G-NH(2) (Baby L9C) is derived by global analysis. The mechanism involves rapid initial collapse of two peptides by Hg(II) forming Hg(Baby L9C(-H))(2) with a linear thiolato Hg(II) bound to the cysteine sulfur atoms. Here, Baby L9C(-H) denotes Baby L9C with the cysteine thiol deprotonated. Addition of the third peptide, forming the three-stranded coiled coil, is the rate-determining step and results in an intermediate state involving two separate species. One of the species, termed the properly folded intermediate, undergoes rapid deprotonation of the third cysteine thiol, yielding the desired three-stranded coiled coil with an encapsulated trigonal thiolato Hg(II). The other species, termed the misfolded intermediate, rearranges in an experimentally distinguishable step to the properly folded intermediate. The order of the reaction involving the addition of the third peptide with respect to the concentration of Baby L9C indicates that addition of the third helix only occurs through reaction of Hg(Baby L9C(-H))(2) and Baby L9C that is unassociated with a coiled coil. Temperature dependence of the reaction afforded activation parameters for both the addition of the third helix (deltaH = 20(2) kcalmol; deltaS= 40(5) calmol K) and the rearrangement of the misfolded intermediate steps (deltaH = 23(2) kcalmol; deltaS= 27(5) calmol K). The mechanism is discussed with regard to metalloprotein folding and metalloprotein design.
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