This paper presents a new azo dye 3-[2-(1H-indol-2-yl)ethyldiazenyl]quinolin-2-ol] from the reaction of the diazonium salt derived from tryptamine and 2-hydroxyquinoline. Azo dye was used to prepare a series of complexes with the chlorides of Ni(II), Pt(IV), Pd(II), Cd(II), and Zn(II). Compounds were analyzed and characterized using elemental analysis, magnetic measurement, UV-vis, IR, MS, NMR, and conductivity. The findings demonstrated that the ligand acts as ionic in complex form, O-bidentate, supporting the proposed formula. The complexes generally exhibited tetrahedral and octahedral geometries, except the palladium complex, which adopted a square planar geometry. TGA was used to investigate the thermal characteristics of compo

New Azo ligands HL1 [2-Hydroxy-3-((5-mercapto-1,3,4-thiadiazol-2-yl)diazenyl)-1-naphth aldehyde] and HL2 [3-((1,5-Dimethyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-yl)diazenyl)-2-hydroxy-1-naphthaldehyde] have been synthesized from reaction (2-hydroxy-1-naphthaldehyde) and (5-amino-1,3,4-thiadiazole-2-thiol) for HL1 and (4-amino-1,5-dimethyl-2-phenyl-1H-pyrazol-3(2H)-one) for HL2. Then, its metal ions complexes are synthesized with the general formula; [CrHL1Cl3(H2O)], [VOHL1(SO4)] [ML1Cl(H2O)] where M = Mn(II), Co(II), Ni(II) and Cu(II), and general formula; [Cr(L2)2 ]Cl and [M(L2)2] where M = VO(II), Mn(II), Co(II), Ni(II) and Cu(II) are reported. The ligands and their metal complexes are characterized by phisco- chemical spectroscopic

The hydroisomerization of n-decane was studied on SAPO-11 catalyst. Catalyst of 0.25wt.%Pt/SAPO-11 was prepared locally and used in the present work. The hydroconversion performed in a continuous fixed-bed laboratory reaction unit. Experiments of n-decane isomerization were performed in a temperature range of 200 to 275°C,LHSV range of 0.5-2 h-1, and hydrogen to decane mole ratio of 2.1-8.2. The results show that the n-decane conversion increases with increasing temperature and  decreasing LHSV , the maximum conversion 56.77 % was achieved at temperature 275°C and LHSV of 0.5 h-1. The kinetic of n-decane isomerization was also studied and the reaction was first order. The kinetic analysis also showed that the activation energy eq

The hydroisomerization of n-decane was studied on SAPO-11 catalyst. Catalyst of 0.25wt.%Pt/SAPO-11 was prepared locally and used in the present work. The hydroconversion performed in a continuous fixed-bed laboratory reaction unit. Experiments of n-decane isomerization were performed in a temperature range of 200 to 275°C,LHSV range of 0.5-2 h^-1, and hydrogen to decane mole ratio of 2.1-8.2. The results show that the n-decane conversion increases with increasing temperature and  decreasing LHSV , the maximum conversion 56.77 % was achieved at temperature 275°C and LHSV of 0.5 h^-1. The kinetic of n-decane isomerization was also studied and the reaction was first order. The kinetic analysis also showed that the

sanaa tareq, Baghdad Science Journal, - Cited by 1

Some physical properties enthalpy (?H), entropy (?s), free energy (?G),capacities(?cp?) and Pka values) for valine in dimethyl foramideover the temperature range 293.15-318.15K, were determined by direct conductance measurements. The acid dissociation at six temperature was examined at solvent composition x2) involving 0.141 of dimethyl foramide . As results, calculated values have been used to determine the dissociation constant and the associated thermodynamic function for the valine in the solvent mixture over temperatures in the range 293.15-318.15 k. The Pka1, and Pka2 were increased with increasing temperature.

Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and BC

Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and B