ArticleChemistry (Weinheim an der Bergstrasse, Germany)2012
The importance of stereochemically active lone pairs for influencing Pb(II) and As(III) protein binding.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- Single stereocenter inversion of a cyclic tetrapeptide enables the detoxification of lead-exposed mice.Chemical science · 2026Article
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
- Synthesis and structural characterization of the heavy tricysteinylpnictines, models of protein-bound As(III), Sb(III), and Bi(III).Dalton transactions (Cambridge, England : 2003) · 2024Article
- AsJournal of the American Chemical Society · 2024Article
- Macrobicyclic Dibridgehead Di(trialkyl)pnictogens E((CHOrganometallics · 2024Article
- Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsSInorganic chemistry · 2023Article
- Pb(II) coordination to the nonclassical zinc finger tristetraprolin: retained function with an altered fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Review
- The Pnictogen Bond: The Covalently Bound Arsenic Atom in Molecular Entities in Crystals as a Pnictogen Bond Donor.Molecules (Basel, Switzerland) · 2022Review
- Location-Dependent Lanthanide Selectivity Engineered into Structurally Characterized Designed Coiled Coils.Angewandte Chemie (International ed. in English) · 2021Article
- Open Reading Frame 1 Protein of the Human Long Interspersed Nuclear Element 1 Retrotransposon Binds Multiple Equivalents of Lead.Journal of the American Chemical Society · 2021Article
- 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
- 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
- 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
- Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy Metals.Biochemistry · 2015Article
- Sculpting Metal-binding Environments inIsrael journal of chemistry · 2015Article
- Are delta-aminolevulinate dehydratase inhibition and metal concentrations additional factors for the age-related cognitive decline?International journal of environmental research and public health · 2014Article
- The influence of the occupational exposure to heavy metals and tobacco smoke on the selected oxidative stress markers in smelters.Biological trace element research · 2014Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The toxicity of heavy metals, which is associated with the high affinity of the metals for thiolate rich proteins, constitutes a problem worldwide. However, despite this tremendous toxicity concern, the binding mode of As(III) and Pb(II) to proteins is poorly understood. To clarify the requirements for toxic metal binding to metalloregulatory sensor proteins such as As(III) in ArsR/ArsD and Pb(II) in PbrR or replacing Zn(II) in δ-aminolevulinc acid dehydratase (ALAD), we have employed computational and experimental methods examining the binding of these heavy metals to designed peptide models. The computational results show that the mode of coordination of As(III) and Pb(II) is greatly influenced by the steric bulk within the second coordination environment of the metal. The proposed basis of this selectivity is the large size of the ion and, most important, the influence of the stereochemically active lone pair in hemidirected complexes of the metal ion as being crucial. The experimental data show that switching a bulky leucine layer above the metal binding site by a smaller alanine residue enhances the Pb(II) binding affinity by a factor of five, thus supporting experimentally the hypothesis of lone pair steric hindrance. These complementary approaches demonstrate the potential importance of a stereochemically active lone pair as a metal recognition mode in proteins and, specifically, how the second coordination sphere environment affects the affinity and selectivity of protein targets by certain toxic ions.
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