29 research outputs found
Oxidation of benzoin catalyzed by oxovanadium (IV) schiff base complexes
BACKGROUND: The oxidative transformation of benzoin to benzil has been accomplished by the use of a wide
variety of reagents or catalysts and different reaction procedures. The conventional oxidizing agents yielded mainly
benzaldehyde or/and benzoic acid and only a trace amount of benzil. The limits of practical utilization of these
reagents involves the use of stoichiometric amounts of corrosive acids or toxic metallic reagents, which in turn
produce undesirable waste materials and required high reaction temperatures.
In recent years, vanadium complexes have attracted much attention for their potential utility as catalysts for various
types of reactions.
RESULTS: Active and selective catalytic systems of new unsymmetrical oxovanadium(IV) Schiff base complexes for
the oxidation of benzoin is reported. The Schiff base ligands are derived between 2-aminoethanol and 2-hydroxy-1-
naphthaldehyde (H2L1) or 3-ethoxy salicylaldehyde (H2L3); and 2-aminophenol and 3-ethoxysalicylaldehyde (H2L2) or
2-hydroxy-1-naphthaldehyde (H2L4). The unsymmetrical Schiff bases behave as tridentate dibasic ONO donor
ligands. Reaction of these Schiff base ligands with oxovanadyl sulphate afforded the mononuclear oxovanadium(IV)
complexes (VIVOLx.H2O), which are characterized by various physico-chemical techniques.
The catalytic oxidation activities of these complexes for benzoin were evaluated using H2O2 as an oxidant. The best
reaction conditions are obtained by considering the effect of solvent, reaction time and temperature. Under the
optimized reaction conditions, VOL4 catalyst showed high conversion (>99%) with excellent selectivity to benzil
(~100%) in a shorter reaction time compared to the other catalysts considered.
CONCLUSION: Four tridentate ONO type Schiff base ligands were synthesized. Complexation of these ligands with
vanadyl(IV) sulphate leads to the formation of new oxovanadium(IV) complexes of type VIVOL.H2O.
Elemental analyses and spectral data of the free ligands and their oxovanadium(IV) complexes were found to be in
good agreement with their structures, indicating high purity of all the compounds.
Oxovanadium complexes were screened for the oxidation of benzoin to benzil using H2O2 as oxidant. The effect of
time, solvent and temperature were optimized to obtain maximum yield. The catalytic activity results demonstrate
that these catalytic systems are both highly active and selective for the oxidation of benzoin under mild reaction
conditions.Web of Scienc
Correspondence of gradual developmental increases of expression of galectin-reactive glycoconjugates with alterations of the total contents of the two differentially regulated galectins in chicken intestine and liver as indication for overlapping function
The duplication of genes for recognition molecules and the ensuing diversification of the members of such families generate complex groups of homologous proteins. One example are galactosidespecific lectins whose sequences display constant features related to sugar binding, the galectins. Based on the inverse abundance of the chicken galectins CG-14 and CG-16 in adult intestine and liver, these two lectins represent a model to comparatively study expression of the related proteins and the galectin-reactive sites (glycoproteins and glycolipids) biochemically and histochemically. Functional overlap andtor acquisition of distinct functions would be reflected in qualitative andlor quantitative aspects of ligand display. Using five different stages of embryogenesis, differential regulation of the two galectins was detected in liver and intestine. The clear preference for one galectin (CC-14) was observed in intestine already at rather early stages, whereas equivalence for both proteins was noted in liver from day 12 to day 18 prior to hatching, as seen by ELISA assays and Western blot analysis. Presentation of galectin-reactive glycoproteins showed a tendency for gradual increase in both organs. Galectin-blotting analysis revealed primarily very similar patterns of positive bands at the different stages of development and only few quantitative and qualitative changes. The reactivity of glycolipids in a solid-phase assay was more variable, even surpassing the response of extracts of the adult organ at several embryonic stages. While the localization patterns of the galectins and galectinreactive sites were nearly indistinguishable in the liver, intestinal tissue differed with respect to the placement and accessibility of binding sites. Thus, the results suggest a differential regulation of galectin activities in the two organs. As a sum they resemble the course of development of availability of glycoprotein ligands in vitro. These findings support the notion for a partial functional redundancy in this family. The described approach to employ galectin-specific antibodies and the labeled galectins as tools to assess presentation of ligands is suggested to be of general relevance to address the question of distinct vs. overlapping functions of related recognition molecules
Crystal Structure of 4-{[(1E)-(3,5-dinitro-2-hydroxyphenyl)-methylidene]amino}-1,5-dimethyl-2-phenyl-2,3-dihydro-1H-pyrazol-3-oneacetonitrile.
Crystal Structure Of 1-[N-(6-Methyl-2-Pyridyl)Aminomethylidene] 2(1H)-Naphthalenone
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