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An enolato-bridged dinuclear Cu(II) complex with a coumarin-assisted precursor: a spectral, magnetic and biological study

Das, Kuheli and Panda, Uttam and Datta, Amitabha and Roy, Suman and Mondal, Sudipa and Massera, Chiara and Askun, Tulin and Celikboyun, Pinar and Garribba, Eugenio and Sinha, Chittaranjan and Anand, Kushi and Akitsu, Takashiro and Kobayashi, Kana (2015) An enolato-bridged dinuclear Cu(II) complex with a coumarin-assisted precursor: a spectral, magnetic and biological study. In: NEW JOURNAL OF CHEMISTRY, 39 (9). pp. 7309-7321.

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Official URL: http://dx.doi.org/10.1039/c5nj00789e

Abstract

A new, phenoxo-bridged Cu-II dinuclear complex Cu-2(L)(2)(DMF)(2)] (1) has been obtained by employing the coumarin-assisted tridentate precursor, H2L, benzoic acid(7-hydroxy-4-methyl-2-oxo-2H-chromen-8-ylmethylene)-hydrazide]. Complex 1 has been systematically characterized by FTIR, UV-Vis, fluorescence and PR spectrometry. The single crystal X-ray diffraction analysis of 1 shows that the geometry around each copper ion is square pyramidal, comprising two enolato oxygen atoms belonging to different ligands (which assemble the dimer bridging the two metal centers), one imine-N and one phenolic-O atoms of the Schiff base and one oxygen atom from the DMF molecule. The temperature dependent magnetic interpretation agrees with the existence of weak ferromagnetic interactions between the bridging dinuclear Cu(II) ions. Both the ligand and complex 1 exhibit anti-mycobacterial activity and considerable efficacy towards M. tuberculosis H37Rv ATCC 27294 and M. tuberculosis H37Ra ATCC 25177 strains. The cytotoxicity study on human adenocarcinoma cell lines (MCF7) suggests that the ligand and complex 1 have potential anticancer properties. Molecular docking of H2L with the enoyl acyl carrier protein reductase of M. tuberculosis H37R(v) (PDB ID: 4U0K) is examined and the best docked pose of H2L shows one hydrogen bond with Thr196 (1.99 angstrom).

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the ROYAL SOC CHEMISTRY, THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Department/Centre: Division of Biological Sciences > Biochemistry
Depositing User: Id for Latest eprints
Date Deposited: 09 Oct 2015 05:33
Last Modified: 09 Oct 2015 05:33
URI: http://eprints.iisc.ac.in/id/eprint/52521

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