Synthesis and structure of tetranuclear zinc(II) and binuclear copper(II) complexes of a dithiolate compartmental macrocyclic ligand: A model for the binuclear CuA site in cytochrome c oxidase and N2O reductase

The tetranuclear cluster [Zn2L(µ-OH)]2[ClO4]2·2H2O (L = dianion of the condensation product of 1,3-diaminopropane and 2,6-diformyl-4-methylthiophenol) shows two unique dinuclear ZnII units linked by two µ-hydroxy bridges; the structure of the CuII complex [Cu2L(HOMe)2](NO3)]PF6 shows square-pyramidal coordination at the Cu centres with two thiolate bridges and two terminal N-donors, with a Cu⋯Cu separation of 3.264(2)A.

[1]  P. K. Bharadwaj,et al.  Crystal structure and magnetic properties of the cluster complex tris(1-cysteinethiolato)pentacopper(2+) perchlorate monohydrate, a mixed-valence copper-mercaptide species , 1986 .

[2]  J. Beckman,et al.  Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite. , 1995, Biochemistry.

[3]  W. Kaim,et al.  The Dinuclear CuA Center in Cytochrome c Oxidase and N2O Reductase—A Metal–Metal Bond in Biology? , 1995 .

[4]  Hartmut Michel,et al.  Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans , 1995, Nature.

[5]  Jason A. Halfen,et al.  Structural Characterization of the First Example of a Bis(μ-thiolato)dicopper(II) Complex, Relevance to Proposals for the Electron Transfer Sites in Cytochrome c Oxidase and Nitrous Oxide Reductase , 1995 .

[6]  W. Tolman,et al.  Mixed Valence, Tricopper(I,II,I) Complexes with Thiolate Bridges. Progress toward Synthetic Models of the Putative {Cu2}3+ Sites in Nitrous Oxide Reductase and Cytochrome c Oxidase , 1995 .

[7]  A. J. Blake,et al.  Schiff-base compartmental macrocyclic complexes , 1996 .

[8]  William B. Tolman,et al.  A thiolate-bridged, fully delocalized mixed-valence dicopper(I,II) complex that models the CuA biological electron-transfer site , 1996 .

[9]  I. Dance,et al.  The crystal and molecular structure of the hexa-(μ2-benzenethiolato)tetracuprate(I) dianion , 1976 .

[10]  D. M. Grove,et al.  Novel trinuclear and hexanuclear heteroorganocopper compounds with phosphine ligands, bridging alkynyls, and intramolecularly coordinating bridging arylthiolates : X-ray structures of [Cu3{SC6H4(CH(R)NMe2)-2}2-(C_Ct-Bu)]2 (R = H, Me) , 1992 .

[11]  G. Matsubayashi,et al.  The first dinuclear copper(II) complex bridged by a single thiolate-sulphur atom: synthesis, properties, and structure , 1985 .

[12]  D. M. Grove,et al.  A New Class of Organocopper and Organocuprate Compounds Derived from Copper( I) Arenethiolates , 1992 .

[13]  W. Lipscomb,et al.  Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. , 1992, Journal of molecular biology.

[14]  W. Lipscomb,et al.  Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography. , 1995, Biochemistry.

[15]  C. Rao,et al.  Synthesis and structural systematics of ethane-1,2-dithiolato complexes , 1986 .

[16]  A. Blake,et al.  Polynuclear nickel(II) complexes of N4O2- and N4S2-compartmental macrocycles: the structures of a Ni4O4 cubane cluster and the binuclear nickel(II) complex of a benzenethiolate macrocycle , 1993 .

[17]  T. Tomizaki,et al.  Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A , 1995, Science.

[18]  J. Seadon,et al.  The formation and structural chemistry of the hexa(μ- t -butylthiolato) pentacuprate(I) cage anion with triethylammonium and tetraethylammonium cations , 1984 .

[19]  B Chevrier,et al.  Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. , 1994, Structure.

[20]  Jeremy M. Berg,et al.  Ligand variation and metal ion binding specificity in zinc finger peptides , 1993 .

[21]  Michel Frey,et al.  Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas , 1995, Nature.