Geometric preferences in iron(II) and zinc(II) model complexes of peptide deformylase.

A combination of experimental and theoretical studies on (N,S(thiolate))M(II)-formate complexes (M = Fe, Zn) suggests a rationale for the metal ion dependence of peptide deformylase.

A new bis(imidazolyl)(alkylthiolate) tripodal ligand and the spontaneous formation of a disulfide-linked, hydroxo-bridged dinuclear zinc complex.

The new sterically encumbered, tripodal N2S(alkylthiolate) ligand, LIm2SH, has been synthesized and used to prepare [(LIm2S)ZnCH3], which upon protonolysis under acidic conditions leads to the synthesis of a novel dinucleating ligand and a zinc dimer with an unusual structure.

New monomeric cobalt(II) and zinc(II) complexes of a mixed N,S(alkylthiolate) ligand: model complexes of (His)(His)(Cys) metalloprotein active sites.

The new N(2)S(alkylthiolate) ligand 2-methyl-1-[methyl-(2-pyridin-2-ylethyl)amino]propane-2-thiolate, PATH (1), has been prepared and reacted with zinc(II) and cobalt(II) to give the monomeric complexes [(PATH)ZnBr] (2), [(PATH)ZnNCS] (3), [(PATH)CoBr] (4), and [(PATH)CoNCS] (5). The molecular structures of 4 and 5 have been determined by X-ray diffraction. Each complex displays a distorted tetrahedral geometry at the metal center, with the PATH ligand providing the N(2)S(alkylthiolate) donors.