Synthesis and characterization of a newly designed di-copper(II)-based complex and study of its artificial enzyme catalytic activity

Derakhshankhah, H; Saboury, AA; Divsalar, A; Mansouri-Torshizi, H; Bamery, I; Ajloo, D; Moosavi-Movahedi, AA; Hosseinzadeh, R; Ganjali, MR; Ilkhani, H; Khavasi, HR

HERO ID

2841472

Reference Type

Journal Article

Year

2014

HERO ID 2841472
In Press No
Year 2014
Title Synthesis and characterization of a newly designed di-copper(II)-based complex and study of its artificial enzyme catalytic activity
Authors Derakhshankhah, H; Saboury, AA; Divsalar, A; Mansouri-Torshizi, H; Bamery, I; Ajloo, D; Moosavi-Movahedi, AA; Hosseinzadeh, R; Ganjali, MR; Ilkhani, H; Khavasi, HR
Journal Journal of the Iranian Chemical Society
Volume 11
Issue 5
Page Numbers 1381-1390
Abstract A di-copper(II) complex of the formula [(dien)Cu(mu-1,6-DAH)Cu(dien)(NO3)(2)](NO3)(2), where mu-1,6-DAH = 1,6-diaminohexane, has been synthesized and characterized by X-ray crystallography, X-ray powder diffraction, thermal gravimetric (TG) and differential thermal analyses, cyclic voltammetry, infrared, ultraviolet visible spectroscopies and elemental analysis methods. It was crystallized in a monoclinic system, space group P2(1)/n, with a = 8.0297(8) , b = 12.4937(14) , c = 15.3786(15) , beta = 102.739(8) and z = 2. Each copper(II) has a square-based pyramidal coordination geometry with four N atoms building the basal plane (three from dien and one from mu-1,6-DAH). TGA study of the complex revealed the compound to be stable up to 245 A degrees C. Electrochemical behavior of complex and enzyme-like catalytic activity of this complex, as a potential functional model for the active site of tyrosinase, was studied extensively. Kinetic studies show that the complex has the maximum enzymatic activity at pH 8, temperature of 40 A degrees C and ionic strength of 50 mM.
Doi 10.1007/s13738-014-0407-9
Wosid WOS:000341185200018
Is Certified Translation No
Dupe Override No
Is Public Yes
Keyword Bi-copper(II) complex; Artificial tyrosinase; Voltammetiric study; Enzyme kinetic; Dopamine