| pubmed-article:16903704 | pubmed:abstractText | A new N2S(alkylthiolate)-coordinated Pb2+ compound {2-methyl-1-[methyl(2-pyridin-2-ylethyl)amino]propane-2-thiolatolead perchlorate, [PATH-Pb][ClO4]} has been synthesized and characterized by X-ray diffraction and by 207Pb NMR. [PATH-Pb]+ is the first reported three-coordinate Pb complex with an alkanethiolate ligand and, hence, is a good model for Pb-cysteine interactions in proteins. The Pb center displays distorted trigonal-planar geometry. The Pb-S bond lengths are extremely short (2.590(10) and 2.597(10) A for two distinct monomers in the unit cell). 207Pb NMR revealed a Pb resonance at 5318 ppm, much further downfield than Pb complexes with N and O ligation. Given recent evidence of three-coordinate Pb-binding in proteins with cysteine-rich metal-binding sites, [PATH-Pb]+ is an important model for Pb sites in biological systems. Crystal data: C12H19N2SPbClO4, Mr = 529.99, monoclinic, P2(1)/n, a = 16.8297(9) A, b = 11.9719(6) A, c = 17.0868(9) A, V = 3237.7(3) A3, and Z = 8. | lld:pubmed |
