Synthesis, characterization, X-ray molecular structure and catalase-like activity of a non-heme iron complex:: Dichloro[N-propanoate-N,N-bis-(2-pyridylmethyl)amine]iron(III)

被引:29
作者
Carvalho, Nakedia M. F.
Horn, Adolfo, Jr.
Faria, Roberto B.
Bortoluzzi, Adailton J.
Drago, Valderes
Antunes, O. A. C.
机构
[1] Univ Fed Rio de Janeiro, Inst Quim, BR-21945970 Rio De Janeiro, Brazil
[2] Univ Estadual Norte Fluminense, Lab Ciencias Quim, BR-28013600 Rio De Janeiro, Brazil
[3] Univ Fed Santa Catarina, Dept Quim, BR-88040900 Florianopolis, SC, Brazil
[4] Univ Fed Santa Catarina, Dept Fis, BR-88040900 Florianopolis, SC, Brazil
关键词
catalase-like activity; kinetic studies; iron(III) complex; crystal structure;
D O I
10.1016/j.ica.2006.06.021
中图分类号
O61 [无机化学];
学科分类号
070301 ; 081704 ;
摘要
In this work we present the synthesis and characterization of the complex dichloro[N-propanoate-N,N-bis-(2-pyridylmethyl)amine]iron(III) [Fe-III(PBMPA)Cl-2]. The ligand LiPBMPA was synthesized through the Michael reaction of BMPA with methylacrylate, followed by alkaline hydrolysis. The complex [Fe-III(PBMPA)Cl-2] has been synthesized by the reaction of the ligand with FeCl3 center dot H2O and was mainly characterized by cyclic voltammetry, conductivimetry, and electronic, infrared and Mossbauer spectroscopies, and by X-ray structural analysis, which showed an iron center coordinated by one carboxylate oxygen in a monodentate way, one tertiary amine, two pyridine groups and two chloride ions. It has been proposed that in water the chloride ligands are shifted by the solvent molecules and the species [Fe-III(PBMPA)(H2O)(2)]Cl-2 is predominant. The catalase-like activity of the complex was tested in water, and it proved to be active in the hydrogen peroxide dismutation. Kinetics studies were conducted following the initial rates method. The reaction is first order in relation to both the complex and the hydrogen peroxide. Based on the presence of a lag phase that depends on the initial complex concentration, we propose that the active species that shows in situ catalase-like activity, is a binuclear complex. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:4250 / 4258
页数:9
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