%0 Journal Article
%T Synthesis, CP-MAS NMR Characterization, and Antibacterial Activities of Glycine and Histidine Complexes of Cd(SeCN)2 and Hg(SeCN)2
%A Bassem A. Al-Maythalony
%A M. Monim-ul-Mehboob
%A Mohammed I. M. Wazeer
%A Anvarhusein A. Isab
%A M. Nasiruzzaman Shaikh
%A Saleh Altuwaijri
%J Bioinorganic Chemistry and Applications
%D 2013
%I Hindawi Publishing Corporation
%R 10.1155/2013/476874
%X The synthesis and characterization of cadmium and mercury complexes of selenocyanate of the type [(L)M(SeCN)2] are described, where L is L-Histidine (His) or L-Glycine (Gly) and M is Cd2+ or Hg2+. These complexes are obtained by the reaction of 1 equivalent of respective amino acids with metal diselenocyanate precursor in a mixture of solvents (methanol£¿:£¿water = 1£¿:£¿1). These synthesized compounds are characterized by analytical and various spectroscopic techniques such as elemental analysis (EA), IR, and NMR in solution and in the solid state for and . The in vitro antibacterial activities of these complexes have been investigated with standard type cultures of Escherichia coli (MTCC 443), Klebsiella pneumoniae (MTCC 109), Pseudomonas aeruginosa (MTCC 1688), Salmonella typhi (MTCC 733), and Staphylococcus aureus (MTCC 737). 1. Introduction Since the metal ions play vital roles in a number of biological processes such as biomolecules stabilizations, enzyme regulations, transportation of fluids through transmembrane channels, and so forth [1¨C3], numerous metal ions amino acids complexes also act as potent antifungal, antibacterial, and anticancer drugs [4¨C6]. Therefore, the extensive studies of these metallic species have been dedicated to understand the impact on living systems. It is well known that metal-binding proteins cover a large fraction of the total protein, and they are actively participating in several essential life processes [2, 3]. Therefore, understanding of the physicochemical and biochemical properties of metals with amino acids becomes indispensible and a broad area of research for several years [7¨C11]. Among all amino acids found in nature, Histidine is often found as a ligand in various types of metalloenzymes because it is the key amino acids residue in many enzymatic reactions [12]. This is may be due to its stereochemical location of the coordinating atom in Histidine. The Histidine skeleton contains the imidazole side group having two nitrogen atoms capable of participating in metal-ligand coordination sphere thereby it can take on various metal-bound forms in proteins. Thus, it is important to know the coordination modes of the Histidine (His) and Glycine (Gly) ligands to understand the reaction mechanism of metalloenzymes [13]. The coordination modes of various metal ions with amino acids have been the topic of discussion for a long period of time, and the ideas to get the binding modes are not easy to predict for amino acids with large side chain such as Histidine [16], because of different types of donor atoms present in
%U http://www.hindawi.com/journals/bca/2013/476874/