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Synthesis, crystal structures and protease activity of amino acid Schiff base iron(III) complexes

Begum, Mohammed S Ameerunisha and Saha, Sounik and Nethaji, Munirathinam and Chakravarty, Akhil R (2009) Synthesis, crystal structures and protease activity of amino acid Schiff base iron(III) complexes. In: Indian Journal of Chemistry - Section A: Inorganic, Physical, Theoretical and Analytical Chemistry, 48 (4). pp. 473-479.

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Iron(III) complexes, (NHEt3)[Fe(III)(sal-met)(2)] and (NHEt3)[Fe(III)(sal-phe)(2)], of amino acid Schiffbase ligands, viz., N-salicylidene-L-methionine and N-salicylidene L-phenylalanine, have been prepared and their binding to bovine serum albumin (BSA) and photo-induced BSA cleavage activity have been investigated. The complexes are structurally characterized by single crystal X-ray crystallography. The crystal Structures of the discrete mononuclear rnonoanionic complexes show FeN2O4 octahedral coordination geometry in which the tridentate dianionic amino acid Schiff base ligand binds through phenolate and carboxylate oxygen and imine nitrogen atoms. The imine nitrogen atoms are trans to each other. The Fe-O and Fe-N bond distances range between 1.9 and 2.1 angstrom. The sal-met complex has two pendant thiomethyl groups. The high-spin iron(III) complexes (mu(eff) similar to 5.9 mu(B)) exhibit quasi-reversible Fe(III)/Fe(II) redox process near -0.6 V vs. SCE in water. These complexes display a visible electronic hand near 480 nm in tris-HCl buffer assignable to the phenolate-to-iron(III) charge transfer transition. The water soluble complexes bind to BSA giving binding constant values of similar to 10(5) M-1. The Complexes show non-specific oxidative cleavage of BSA protein on photo-irradiation with UV-A light of 365 nm.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to National Institute of Science Communication and Information Resources.
Department/Centre: Division of Chemical Sciences > Inorganic & Physical Chemistry
Depositing User: Ali K S
Date Deposited: 01 Jan 2010 11:19
Last Modified: 26 Feb 2019 08:56
URI: http://eprints.iisc.ac.in/id/eprint/20023

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