Zinc(II) tweezers containing artificial peptides mimicking the active site of phosphotriesterase: The catalyzed hydrolysis of the toxic organophosphate parathion |
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Authors: | Mohamed M. Ibrahim Gaber A.M. Mersal |
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Affiliation: | a Chemistry Department, Faculty of Science, Kafr El-Sheikh University, Kafr El-Sheikh 33516, Egyptb Chemistry Department, Faculty of Science, South Valley University, Qena, Egyptc Chemistry Department, Faculty of Science, Taif University, 888 Hawaiya, Saudi Arabia |
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Abstract: | Two new ligand-containing histidine based on N,N′,N″-tris(N-benzyl-l-histidinyl)tri(2-aminoethyl)amine, L1, namely N,N′,N″-tris[(1S)-2-methoxy-2-oxy-1-(1-benzylimidazol-4-ylmethyl)]nitrilotriacetamide L2 and N,N′,N″-tris{N-benzyl-N-[N-benzyl-N-(N-benzyl-l-histidinyl)-l-histidinyl]-l-histidinyl}tri(2-aminoethyl)amine L3 were prepared. Zinc(II) binding studies by these ligand systems were analyzed by means of potentiometric and 1H NMR titrations in aqueous methanol (33 % v/v). Subsequently their zinc(II) complexes [L1Zn(H2O)](ClO4)2·HClO4 (1), [L2Zn(OH2)](ClO4)2·H2O (2), and ([L3Zn3(H2O)3](ClO4)6·3HClO4·5H2O (3), respectively were synthesized and characterized. The reactivity of the trinuclear complex (3) toward the hydrolysis of the toxic organophosphate parathion was investigated and compared with that of the mononuclear reference complex (1). From the pH dependence of the apparent rate constants, and the deprotonation constant (pKa) of the coordinated water molecules in (1), the active species were confirmed to be {[HL1Zn(OH)]2+/[L1Zn(H2O)]2+} at pH 8.5. The trizinc complex (3) effects hydrolysis of parathion, with three times rate enhancement over the mononuclear (1), indicating that cooperative action of the three zinc centers is limited. |
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Keywords: | Syntheses Artificial peptides Trinuclear zinc(II) complex Modeling Parathion Detoxification |
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