Abstract
The title compound, [Cu2(C19H23N7O)(C2H3O2)4] n , was obtained via reaction of copper(II) acetate with the coordinating ligand, 6-eth-oxy-N 2,N 4-bis-[2-(pyridin-2-yl)eth-yl]-1,3,5-triazine-2,4-di-amine. The crystallized product adopts the monoclinic P21/c space group. The metal core exhibits a paddle-wheel structure typical for dicopper tetra-acetate units, with triazine and pyridyl nitro-gen atoms from different ligands coordinating to the two axial positions of the paddle wheel in an asymmetric manner. This forms a coordination polymer with the segments of the polymer created by the c-glide of the P21/c setting of the space group. The resulting chains running along the c-axis direction are held together by intra-molecular N-H⋯O hydrogen bonding. These chains are further packed by dispersion forces, producing an extended three-dimensional structure.
Highlights
The title compound, [Cu2(C19H23N7O)(C2H3O2)4]n, was obtained via reaction of copper(II) acetate with the coordinating ligand, 6-ethoxy-N2,N4-bis[2-(pyridin2-yl)ethyl]-1,3,5-triazine-2,4-diamine
The metal core exhibits a paddle-wheel structure typical for dicopper tetraacetate units, with triazine and pyridyl nitrogen atoms from different ligands coordinating to the two axial positions of the paddle wheel in an asymmetric manner
A well-known series of metalloenyzmes containing dinuclear copper active sites is that of the polyphenol oxidases where the catechol is oxidized to quinone products (Ravikiran & Mahalakshmi, 2014)
Summary
Dinuclear CuII groups are recognized for their crucial role as active sites in metalloenzymes and are present in many biological systems (Festa & Thiele, 2011; Solomon et al, 2014). There has been an increased effort to carry over this efficient and selective oxidation into biomimetic models of metalloenzymes (Mahadevan et al, 2000; Panda et al, 2011; Marion et al, 2012) As part of this quest, significant efforts have been made to identify and better understand the specific structural patterns found at these copper-containing active sites. When designing mimics of catechol oxidase, many model catalysts include the same basic structural elements (Koval et al, 2006) These models often contain multidentate ligands with at least five coordinating heteroatoms branched off a central ring, all coordinating to the copper centers. Additional coordination by the terminal pendant pyridine group on the ligand to another copper paddle-wheel unit creates a continuous coordinated chain linkage
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