title: Covalent linkage of the type-2 and type-3 structural mimics to model the active site structure of multicopper oxidases: synthesis and magneto- structural properties of two angular trinuclear copper(II) complexes.
abstract: Two new angular trinuclear copper(II) complexes of formulation [Cu(3)(HL)LL'](ClO(4)), where L' is imidazole (Him, 1) or 1-methylimidazole (1-MeIm, 2) and H(3)L is a Schiff base obtained from the condensation of salicylaldehyde and 1,3-diaminopropan-2-ol (2:1 mole ratio), are prepared from a reaction of [Cu(2)L(mu-Br)] and [Cu(HL)] in the presence of L' and isolated as perchlorate salts. The crystal structures of 1 and 2 consist of a trinuclear copper(II) unit formed by the covalent linkage of monomeric type-2 mimic and dimeric type-3 mimic precursor complexes to give an angular arrangement of the metal atoms in the core which is a model for the active site structure of blue multicopper oxidases. In 1 and 2, the coordination geometry of two terminal copper atoms is distorted square-planar. The central copper has a distorted square-pyramidal (4 + 1) geometry. The mean Cu...Cu distance is approximately 3.3 A. The complex has a diphenoxo-bridged dicopper(II) unit with the phenoxo oxygen atoms showing a planar geometry. In addition, the complex has an endogenous alkoxo-bridged dicopper(II) unit showing a pyramidal geometry for the oxygen atom. The 1:1 electrolytic complexes show a d-d band at 607 nm. Cyclic voltammetry of the complexes in MeCN containing 0.1 M TBAP using a glassy carbon working electrode displays a Cu(3)(II)/Cu(2)(II)Cu(I) couple near -1.0 V (vs SCE). The variable temperature magnetic susceptibility measurements in the range 300-18 K show antiferromagnetic coupling in the complexes giving magnetic moments of approximately 3.0 mu(B) at 300 K and approximately 2.1 mu(B) at 18 K for the tricopper(II) unit. The experimental susceptibility data are theoretically fitted using a model with Heisenberg spin-(1)/(2) Hamiltonian for a trimer of spin-(1)/(2) copper(II) ions having two exchange parameters involving the alkoxo-bridged dicopper(II) (J1) and the diphenoxo-bridged dicopper(II) (J2) units, giving J1 and J2 values of -82.7, -73 cm(-1) for 1 and -98.3, -46.1 cm(-1) for 2, respectively. The structural features indicate a higher magnitude of anitiferromagnetic coupling in the alkoxo-bridged unit based on the greater value of the Cu-O-Cu angle in comparison to the diphenoxo-bridged unit. The core structures of 1 and 2 compare well with the first generation model complexes for the active site structure of multicopper oxidases in the oxidized form. The crystal structure of 1 exhibits a lamellar structure with a gap of approximately 7 A containing water molecules in the interlamellar space. Complex 2 forms a hexanuclear species due to intermolecular hydrogen bonding interactions involving two trimeric units. The crystal packing diagram of 2 displays formation of a three-dimensional framework with cavities containing the perchlorate anions.
authors.affiliation: Department of Inorganic and Physical Chemistry, Indian Institute of Science, Bangalore-560012, India.
authors.forename: Arindam
authors.initials: A
authors.lastname: Mukherjee
authors.forename: Indranil
authors.initials: I
authors.lastname: Rudra
authors.forename: Sunil G
authors.initials: SG
authors.lastname: Naik
authors.forename: Suryanarayanasastry
authors.initials: S
authors.lastname: Ramasesha
authors.forename: Munirathinam
authors.initials: M
authors.lastname: Nethaji
authors.forename: Akhil R
authors.initials: AR
authors.lastname: Chakravarty
mesh_terms: D000465:Algorithms; D003300:Copper / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D007202:Indicators and Reagents; D008280:Magnetics; D008958:Models, Molecular; D008968:Molecular Conformation; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D010088:Oxidoreductases / Q000737:chemistry*; D013696:Temperature
chemical_list: D007202:Indicators and Reagents; D009942:Organometallic Compounds; D003300:Copper; D010088:Oxidoreductases