Syntheses and Characterization of Fe(II) and Cu(I) Complexes Supported by a P2S2 Tetradentate ligand; Biomimetic Complex of Fe-only Hydrogenase

Abstract

Our research team has been interested in studying the roles of metal sites in metalloproteins Metal centers with sulfur-rich coordination sphere are present in many metalloproteins such as hydrogenase CO dehydrogenase and Metallothioneins Therefore we have focused on studying chemistry of metal complexes with sulfur ligation environment to provide the fundamental understanding for the nature of metal sites in biological systems In this research a new type of thiolate ligand tetradentate diphosphine-dithiolate has been developed Several metal complexes of this ligand have also been studied In this thesis the syntheses of the diphosphine-dithiolate ligand H2[P2S2*] are described Several physical methods have been applied to characterize the obtained ligand Two metal complexes of P2S2* derivatives [Fe(P2S2*)(CO)2] and [Cu2(P2S2*)(PPh3)4]‧4CH3OH‧H2O are also synthesized and characterized by X-ray crystallography and spectroscopies [Fe(P2S2*)(CO)2] is a monoiron(II) species The metal center adopts an octahedral geometry by binding to a P2S2* ligand and two carbonyl ligands [Cu2(P2S2*)(PPh3)4]‧4CH3OH‧H2O consists of a dimeric unit and embraces a crystallographic inversion center Each Cu(I) has a tetrahedral geometry and the coordination sphere is completed by one thiolato group and one phosphine atom of P2S2* ligand as well as two phosphine atoms from two PPh3 ligands

Date of Award	2015 Aug 6
Original language	English
Supervisor	Konopka Richard L. (Supervisor)