Glyoxal-promoted homogeneous catalytic oxygenation of cyclohexane with hydrogen peroxide in the presence of V and Co compounds

The efficiency of cyclohexane oxidation with hydrogen peroxide catalyzed by vanadyl acetylacetonate at 40 °C and atmospheric pressure is enhanced by glyoxal additive. The process selectively produces a mixture of cyclohexyl hydroperoxide, cyclohexanol, and cyclohexanone with a high rate (up to 4400 catalyst turnover number). Cobalt(II) acetylacetonate is much less active but more selective with respect to cyclohexyl hydroperoxide.__________Published in Russian in Izvestiya Akademii Nauk. Seriya Khimicheskaya, No. 2, pp. 307–310, February, 2005.     

Liquid-phase oxidation of anthracene by hydrogen peroxide in the presence of heterogenized vanadyl acetylacetonate

The synthesis of heterogenized vanadyl acetylacetonate was accomplished by alkylation of a chloromethylated styrene—divinylbenzene copolymer via activation by Co(II) complexes. The effect of heterogenization on the structure of the complexes and their catalytic properties in the peroxide oxidation of anthracene was investigated by kinetic studies and EPR spectroscopy. Increased stability during oxidation of the catalytic centers of the polymer sample as compared with homogeneous vanadyl acetylacetonate was demonstrated.Department of Fine Organic Synthesis, Institute of Chemistry, Bashkir Science Center, Ural Branch, Russian Academy of Sciences, Ekaterinburg 620219. Translated from Izvestiya Akademii Nauk, Seriya Khimicheskaya, No. 4, pp. 800–804, April, 1992.     

PYRIDINETHIONES PREPARATION AND CHEMISTRY OF 1-SUBSTITUTED-2-FORMYL-2(1H)-PYRIDINETHIONES AND -SELONES

Abstract

Ring closure reactions of glutacondialdehyde derivatives have been reported. We have reported the synthesis of 1-substituted-3-formyl-2(1H)-pyridinethiones 2 from the glutacondialdehyde anion 1 and isothiocyanates.     

Concomitant reduction of dimethylformamide and oxidation of vanadyl sulfate to N,N′-dimethylammonium decavanadate cluster and DNA,BSA binding,and cytotoxicity (HeLa) studies

Abstract

Several polymetallic anionic clusters display a strong tendency to form robust ion-pairs with appropriate counter cations. We have isolated decavanadate cluster [H₂V₁₀O₂₈]^4– with, hitherto unreported, dimethylammonium ions, [N(CH₃)₂H₂]⁴⁺ as counter cations from vanadyl sulfate and N,N’-dimethylformamide (DMF). It is proposed, for the first time, that dimethylammonium ions are formed by reduction and simultaneous decarboxylation of DMF with oxidation of vanadyl sulfate occurring concomitantly under specified reaction conditions. The different colors observed during the course of the reaction are monitored by UV-Visible spectrophotometry. The structure of isolated cluster compound with four counter cations is confirmed by single crystal X-ray diffraction techniques. The compound is also tested for its DNA/BSA binding efficacy and cytotoxicity on human epitheloid cervix carcinoma (HeLa) cells along with vanadates—vanadium pentoxide and ammonium metavanadate. Based on the results, the cluster shows better IC₅₀ and binding values than vanadates.     

In-vitro antidiabetic activity,theoretical investigation by DFT and molecular docking of mono oxo vanadyl (IV) azomethine macromolecule

Prospective antidiabetic applicant [VO(IV)HBDB] was synthesized qualitatively and rapidly, spending HBDB of the mode N, N′-bis (2-hydroxy benzylidene)-1,2-diaminobenzene/Salophen a well familiar Schiff base with myriad property. Interesting and valuable details of physical and electronic properties, band gap energy, electronic configuration, and NLO possessions of the complex were reported. The complex consent with extraordinary NLO property accords with first-order hyperpolarizability. The impressiveness of the monooxo Vanadyl complex is elevated further by biological applications. The antibacterial evaluation accounts that [VO(IV)HBDB] shows greater activity than HBDB. DPPH scavenging report demonstrates that [VO(IV)HBDB] exhibits greater antioxidant potential than standard assay. Subsequently, in-vitro antidiabetic activity with α-glucosidase enzyme was also excellent. Molecular docking with α-glucosidase protein of PDB id: 3 WY1 illustrates greater binding energy of about −12.3 kcal/mol defined for [VO(IV)HBDB] than HBDB roughly −7.6 kcal/mol with more amino acid binding residues. The above-disclosed findings of HBDB and its complex firmly sustenance the biochemists and pharmacological field.