CHEMISTRY Int.J.Curr.Res.Chem.Pharma.Sci.1(4):93-98 © 2014, IJCRCPS. All Rights Reserved 93 RESEARCH ARTICLE SYNTHESIS AND CRYSTAL STRUCTURE OF (BIS [(2-AZANIUMYL-3-METHYLBUTANOYL) OXY]( 2 -BROMANIDYL)FERRIO)- 2 -BROMANIDE M. RADHA RAMANAN 1 , P. GEETHA 2 , R. RADHAKRISHNAN 3 , V. CHITHAMBARAM 2 AND B. GUNASEKARAN 4* 1 Department of Physics, Arasu Engineering College, Kumbakonam, Tamil Nadu, India. 2 Research Centre Physics, Dhanalakshmi College of Engineering, Tambaram, Chennai-600 059 Tamil Nadu, India. 3 PG & Research Department of Physics, Jamal Mohamed College, Tiruchirappalli, Tamil Nadu, India. 4 Department of Physics & Nano Technology, SRM University, SRM Nagar, Kattankulathur, Kancheepuram Dist, Chennai-603 203 Tamil Nadu, India. *Corresponding Author: gunasekaran.b@ktr.srmuniv.ac.in; bguna_sekaran77@yahoo.co.in Introduction Amino acids play central role as building blocks of proteins. Amino acids act not only as the building blocks in protein synthesis but also play a significant role in metabolism. The specific metabolic role of amino acids includes the biosynthesis of polypeptides, proteins and synthesis of nucleotides (Barrett, 1988). The oxidation of amino acids is of interest as different oxidation products are obtained using different oxidants (Laloo and Mahanti, 1990; Annapurna et al., 2008). Valine is one of the 20 proteinogenic (Ambrogelly et al., 2007) amino acid. L-Valine is an essential amino acid classified as non-polar, and forms active sites of enzymes and helps in maintaining proper conformation by keeping them in proper ionic states and wide applications in pharmaceutical and food industry (Bartek et al., 2010). Hence, oxidation of L-Valine may help in understanding some aspects of enzyme kinetics. Valine is a branched-chain amino acid (BCAAs) along with leucine and isoleucine. It is named after the plant valerian. In sickle-cell disease (Platt et al., 1994), valine substitutes for the hydrophilic amino acid glutamic acid in hemoglobin (Bruce et al., 2006). Because valine has large aliphatic hydrophobic side chains (Wang and L. Jiang, 2007), the hemoglobin does not fold correctly. It promotes muscle growth and tissue repair. Many workers (Andreoli, et al., 1984; Saxena and Dhawan, 1983) have studied biologically active metal complexes of amino acids which are important in analytical, biochemical and pharmaceutical fields (Patel, et al., 1996; Khan and P.L. Sahu, 2000; Singh, et al., 1995) and attracted wide attention in different fields of International Journal of Current Research in Chemistry and Pharmaceutical Sciences www.ijcrcps.com Volume 1 Issue: 4 2014 Pages:93-98 (p-ISSN: 2348-5213; e-ISSN: 2348-5221) Abstract The crystal structure of the title compound has been determined by means of X-Ray diffraction. The compound crystallizes in the triclinic space group P1 with a = 6.173 (2) Å, b = 8.202 (3) Å, c = 9.613 (4) Å and = 76.217 (2), = 83.006 (2), = 68.474 (3) º. The terminal methyl groups of L-valine moiety is disordered over two positions with site occupancies of 0.51/0.49 and 0.63/0.37. The crystal packing of the compound is controlled by weak intermolecular C- H…O and N-H…O and N-H…Br interactions. . Keywords: single-crystal X-ray study, L-valine, disorder, R factor = 0.037.