Kinetics and mechanism of the ligand exchange reaction between tetradentate schiff base N,N'-ethylen-bis (salicylaldimine) and Ni(N,N'-propylen-bis(salicylaldimine))

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Kinetics and Mechanism of the Ligand Exchange Reaction Between Tetradentate Schiff Base N,N’-ethylen-bis (salicylaldimine) and Ni(N,N’-propylen-bis(salicylaldimine))

Visible spectrophotometry is used to study the kinetics of ligand exchange in the system Ni(salpn)/H2salen with or without triethylamine (NEt3) and H2O in dimethylformamide (DMF) solvent at 25 ± 0.1 °C and 0.01 M NaNO3 [H2salen and H2salpn are N,N’-ethylen-bis(salicylaldimine) and N,N’-propylen-bis(salicylaldimine), respectively]. It was found that the reaction rate is of the first-order with r...

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Kinetics of the Ligand Exchange Reaction Between Tetradentate Schiff Base N,N'-ethylen-bis (salicylaldimine) and Cu(N,N'-propylen-bis(salicylaldimine)).

Visible spectrophotometry is used to study the kinetic of ligand exchange in the system Cu(salpn)/H2salen with or without triethylamine (NEt3) and H2O in acetonitrile solvent at 25 ± 0.1°C and 0.01 M NaNO3 (H2salen and H2salpn are N,N'-ethylen-bis(salicylaldimine) and N,N'-propylen-bis(salicylaldimine), respectively). It is found that the reaction rate is first-order with respect to Cu(salpn). ...

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Kinetics and mechanism of ligand exchange reaction of copper(II) complexes with tetradentate Schiff base ligands.

The kinetics of a ligand exchange in the CuL4/H2Ln system, where H2Ln is the N,N'-alkylen-bis(salicyldimine) tetradentate Schiff base ligand (n = 2 or 3, CH2 groups in the chain length of the amine backbone) was studied spectrophotometrically in DMF solvent with or without triethylamine (NEt3) and H2O at 25 ± 0.1 °C and an ionic strength of 0.01 M NaNO3. The reaction rate was found to be first-...

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Study the Interaction of Ni Complex of Tetradentate Schiff Base Ligand with HEN Egg White Lysozyme

AbstractInteraction of Ni complex(Salen= N, N´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (HEWL) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. The protein binding affinity of Ni complex was found to be (3.0×103M−1). The binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 M...

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ژورنال

عنوان ژورنال: South African Journal of Chemistry

سال: 2015

ISSN: 1996-840X

DOI: 10.17159/0379-4350/2015/v68a4