{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["29(5)"],"submitter":["Aoun P"],"pubmed_abstract":["In the biomimetic context, many studies have evidenced the importance of the 1<sup>st</sup> and 2<sup>nd</sup> coordination sphere of a metal ion for controlling its properties. Here, we propose to evaluate a yet poorly explored aspect, which is the nature of the cavity that surrounds the metal labile site. Three calix[6]arene-based aza-ligands are compared, that differ only by the nature of cavity walls, anisole, phenol or quinone (L<sup>OMe</sup> , L<sup>OH</sup> and L<sup>Q</sup> ). Monitoring ligand exchange of their Zn<sup>II</sup> complexes evidenced important differences in the metal ion relative affinities for nitriles, halides or carboxylates. It also showed a possible sharp kinetic control on both, metal ion binding and ligand exchange. Hence, this study supports the observations reported on biological systems, highlighting that the substitution of an amino-acid residue of the enzyme active site, at remote distance of the metal ion, can have strong impacts on metal ion lability, substrate/product exchange or selectivity."],"journal":["Chemistry (Weinheim an der Bergstrasse, Germany)"],"pagination":["e202202934"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10107959"],"repository":["biostudies-literature"],"pubmed_title":["Selective Metal-ion Complexation of a Biomimetic Calix[6]arene Funnel Cavity Functionalized with Phenol or Quinone."],"pmcid":["PMC10107959"],"pubmed_authors":["Jabin I","Zhurkin F","Colasson B","Reinaud O","Aoun P","Nyssen N","Richard S"],"additional_accession":[]},"is_claimable":false,"name":"Selective Metal-ion Complexation of a Biomimetic Calix[6]arene Funnel Cavity Functionalized with Phenol or Quinone.","description":"In the biomimetic context, many studies have evidenced the importance of the 1<sup>st</sup> and 2<sup>nd</sup> coordination sphere of a metal ion for controlling its properties. Here, we propose to evaluate a yet poorly explored aspect, which is the nature of the cavity that surrounds the metal labile site. Three calix[6]arene-based aza-ligands are compared, that differ only by the nature of cavity walls, anisole, phenol or quinone (L<sup>OMe</sup> , L<sup>OH</sup> and L<sup>Q</sup> ). Monitoring ligand exchange of their Zn<sup>II</sup> complexes evidenced important differences in the metal ion relative affinities for nitriles, halides or carboxylates. It also showed a possible sharp kinetic control on both, metal ion binding and ligand exchange. Hence, this study supports the observations reported on biological systems, highlighting that the substitution of an amino-acid residue of the enzyme active site, at remote distance of the metal ion, can have strong impacts on metal ion lability, substrate/product exchange or selectivity.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2025-04-27T02:36:29.932Z","creation":"2025-04-06T18:37:59.088Z"},"accession":"S-EPMC10107959","cross_references":{"pubmed":["36321640"],"doi":["10.1002/chem.202202934"]}}