Journal
INORGANIC CHEMISTRY
Volume 52, Issue 6, Pages 2880-2890Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ic302099y
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Funding
- Department of Science and Technology (DST), New Delhi [SR/FT/CS-067/2009]
- University of Kalyani
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Two new water-soluble hetero- and homometallic tetranuclear clusters, Na-4[Cu2Zn2(ccdp)(2)(mu-OH)(2)]center dot CH3OH center dot 6H(2)O (1) and K-3[Cu-4(ccdp)(2)(mu-OH) (mu-OH2)]center dot 14H(2)O (2), have been synthesized in methanol-water at room temperature by exploiting the flexibility, chelating ability, and bridging potential of a carboxylate-rich dinucleating ligand, N,N'-bis(2-carboxybenzomethyl)-N,N'-bis(carboxymethyl)-1,3 diaminopropan-2-ol (H(5)ccdp). Complex 1 is obtained through the self-assembly of two monoanionic [CuZn(ccdp)](-) fragments, which are, in turn, exclusively bridged by two mu-OH- groups. Similarly, complex 2 is formed through the self-assembly of two monoanionic [Cu-2(ccdp)](-) species exclusively bridged by one mu-OH- and one mu-OH2 groups. Complexes 1 and 2 are fully characterized in the solid state as well as in solution using various analytical techniques including a single-crystal X-ray diffraction study. The X-ray crystal structure of 1 reveals that two Cu-II centers are in a distorted square-pyramidal geometry, whereas two Zn-II centers are in a distorted trigonal-bipyramidal geometry. The solid-state structure of 2 contains two dinuclear [Cu-2(ccdp)](-) units having one Cu-II center in a distorted square-pyramidal geometry and another Cu-II center in a distorted trigonal-bipyramidal geometry within each dinuclear unit. In the powder state, the high-field EPR spectrum of complex 1 indicates that two Cu-II ions are not spin-coupled, whereas that of complex 2 exhibits at least one noninteracting Cu-II center coordinated to a nitrogen atom of the ligand. Both complexes are investigated for their binding affinity with the protein bovine serum albumin (BSA) in an aqueous medium at pH similar to 7.2 using fluorescence spectroscopy. Synchronous fluorescence spectra clearly reveal that complexes 1 and 2 bind to the active sites in the protein, indicating that the effect is more pronounced toward tyrosine than tryptophan. Density functional theory calculations have been carried to find the Fukui functions at the metal sites in complexes 1 and 2 to predict the possible metal centers involved in the binding process with BSA protein.
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