Abstract
Two novel coordination compounds, [Zn(L)2(OOCH)2] (1) and [Zn(L)3(OCHO)](OCHO)]·H2O (2) (where L = 2-isopropylimidazole, C6H10N2) have been prepared by reaction of 2-isopropylimidazole with zinc(II) formate at room temperature using toluene as solvent. These compounds were characterized by elemental and thermal analyses, IR, 1HNMR and 13CNMR spectroscopies, single crystal X-ray diffraction and DFT studies. The Zn centers in 1 and 2 adopt pseudo-tetrahedral coordination geometries. Compound 1 crystallizes in the monoclinic system P2/c space group whereas compound 2 crystallizes in the P-1 space group of the triclinic crystal system. Several types of hydrogen intra-/intermolecular interactions are observed in these materials and extend into a two-dimensional leaf like network in 1 and a two-dimensional lattice of rectilinear pillars in 2. Compounds 1 and 2 were also optimized and their frontier molecular orbitals, global reactivity descriptors, molecular electrostatic potential, natural bond orbitals were investigated using density functional theory (DFT). In fact the induced structural differences from complex 1 to complex 2 led to the reduction of the frontier molecular orbital energy gap by 1.338 eV and a decrease of the chemical hardness by 0.669 eV.
Highlights
The synthesis, crystal structures and density functional theory (DFT) studies of two model enzymes, bisformatobis(2-isopropylimidazole)zinc(II), [Zn(N2H10C6)2(OOCH)2] (1) and formatotris(2-isopropylimidazole)Zn(II) formate-water (1/2), [Zn(N2H10C6)3(OCHO)](OCHO)·2H2O (2)
The attempt was successful, the additional presence of one formate counter ion and two hydrated water molecules was observed in the crystal structure of 2
This structural differences induced in these complexes, affected the electronic and physicochemical properties of the complexes
Summary
Zinc complexes have catalytic and structural functions in an estimated 300 enzymes, an example being carboxypeptidase A. This enzyme has been the subject of many recent reviews [4] [5]. Carboxypeptidase A has been used as a model in the development of inhibitor design strategies for medicinal purposes [7] [8] [9] Another well-known zinc enzyme is carbonic anhydrase. Since its discovery in 1932, carbonic anhydrase has been the subject of intense study too [10] It functions primarily in CO2 transport and excretion in blood [10] and is important in photosynthesis because of its ability to convert CO2 to HCO3− reversibly [11]. Biochemical and genetic studies of carbonic anhydrase, analyzed in various tissues of many organs and plant species suggested its effect on a wide range of diverse biological processes, including pH regulation, gas and ion exchange, provision of bicarbonate for anaplerotic reactions, and fatty acid biosynthesis [12]
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