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100-01-6Relevant articles and documents
Development of chemoselective photoreduction of nitro compounds under solar light and blue LED irradiation
Zand, Zahra,Kazemi, Foad,Hosseini, Saber
, p. 338 - 341 (2014)
Solar light and blue light irradiation of the commercially available heterogeneous nano photocatalyst TiO2-P25 leads to reduction of nitro compounds to give the corresponding amines. The methodology provides a green and mild approach to this useful class of organic compounds. Aromatic nitro compounds containing a wide range of functional groups tolerated the conditions to give, chemoselectively the corresponding amines in excellent yields.
Gold catalysts supported on TiO2-nanotubes for the selective hydrogenation of p-substituted nitrobenzenes
Torres, Cecilia C.,Jiménez, Verónica A.,Campos, Cristian H.,Alderete, Joel B.,Dinamarca, Robinson,Bustamente, Tatiana M.,Pawelec, Barbara
, p. 21 - 27 (2018)
Gold nanoparticles supported on titania nanotubes (TiO2NT) were synthesized and employed as an efficient catalysts for the selective hydrogenation of nitrobenzenes. Materials characterization by N2 adsorption-desorption isotherms, XR
A new palladium complex supported on magnetic nanoparticles and applied as an catalyst in amination of aryl halides, Heck and Suzuki reactions
Ghorbani-Choghamarani, Arash,Tahmasbi, Bahman,Noori, Nourolah,Ghafouri-nejad, Raziyeh
, p. 681 - 693 (2017)
A simple, efficient and less expensive protocol for the phosphine-free C–C coupling reactions and synthesis of anilines in the presence of 2-aminobenzamide complex of palladium supported on Fe3O4 magnetic nanoparticles (Pd(0)-ABA-Fe3O4) has been reported. The Suzuki reaction was carried out in water or PEG using phenylboronic acid (PhB(OH)2) or sodium tetraphenyl borate (NaBPh4). Pd(0)-ABA-Fe3O4 has been found promising for Heck reaction of butyl acrylate, styrene or acrylonitrile with aryl halides (including Cl, Br and I). Also, Pd(0)-ABA-Fe3O4 has been found as efficient catalyst for the amination of aryl halides using aqueous ammonia. The products have been obtained in short reaction times and high yields. The catalyst was easily separated using an external magnet from the reaction mixture and reused for several runs without significant loss of its catalytic efficiency or palladium leaching. The leaching of catalyst has been examined by hot filtration and ICP-OES technique. The nanomagnetical catalyst was characterized by FTIR, TGA, XRD, VSM, TEM, SEM, EDS, DLS and ICP-OES techniques.
Purification of an aminopeptidase preferentially releasing N-terminal alanine from cucumber leaves and its identification as a plant aminopeptidase N
Yamauchi, Yasuo,Ejiri, Yukinori,Tanaka, Kiyoshi
, p. 2802 - 2805 (2001)
In this study, a highly active foliar aminopeptidase preferentially releasing N-terminal alanine from artificial substrates was purified and characterized from cucumber (Cucumis sativus L. suyo). The enzyme had a molecular mass of 200 kDa consisting of two subunits of 95 kDa. It was a metalloprotease the pH optimum of which was 8 to 9. It cleaved Ala-, Gly-, Met-, Ser-, Leu-, Lys-, and Arg artificial substrates. An internal amino acid sequence was similar to those of aminopeptidase N (clan MA, family M1) of microorganisms, and was very similar to that of a putative aminopeptidase N of Arabidopsis thaliana. From these results, the highly active aminopeptidase in cucumber leaves was identified to be a plant aminopepitdase N.
Self-protonation upon the electroreduction of 2- and 4-nitrophenylhydroxylamines in aprotic media
Syroeshkin, Mikhail A.,Mendkovich, Andrei S.,Mikhalchenko, Ludmila V.,Rusakov, Alexander I.,Gul'tyai, Vadim P.
, p. 258 - 259 (2009)
Cyclic voltammetry and controlled potential electrolysis were used to show that radical anions of 2- and 4-nitrophenylhydroxylamines electrochemically generated in a 0.1 M Bu4NClO4 solution in DMF undergo protonation with the startin
Structural characterization and function determination of a nonspecific carboxylate esterase from the amidohydrolase superfamily with a promiscuous ability to hydrolyze methylphosphonate esters
Xiang, Dao Feng,Kumaran, Desigan,Swaminathan, Subramanyam,Raushel, Frank M.
, p. 3476 - 3485 (2014)
The uncharacterized protein Rsp3690 from Rhodobacter sphaeroides is a member of the amidohydrolase superfamily of enzymes. In this investigation the gene for Rsp3690 was expressed in Escherichia coli and purified to homogeneity, and the three-dimensional structure was determined to a resolution of 1.8 ? The protein folds as a distorted (β/α)8-barrel, and the subunits associate as a homotetramer. The active site is localized to the C-terminal end of the β-barrel and is highlighted by the formation of a binuclear metal center with two manganese ions that are bridged by Glu-175 and hydroxide. The remaining ligands to the metal center include His-32, His-34, His-207, His-236, and Asp-302. Rsp3690 was shown to catalyze the hydrolysis of a wide variety of carboxylate esters, in addition to organophosphate and organophosphonate esters. The best carboxylate ester substrates identified for Rsp3690 included 2-naphthyl acetate (kcat/Km = 1.0 × 105 M-1 s-1), 2-naphthyl propionate (k cat/Km = 1.5 × 105 M-1 s -1), 1-naphthyl acetate (kcat/Km = 7.5 × 103 M-1 s-1), 4-methylumbelliferyl acetate (kcat/Km = 2.7 × 103 M-1 s-1), 4-nitrophenyl acetate (kcat/Km = 2.3 × 105 M-1 s-1), and 4-nitrophenyl butyrate (kcat/Km = 8.8 × 105 M -1 s-1). The best organophosphonate ester substrates included ethyl 4-nitrophenyl methylphosphonate (kcat/Km = 3.8 × 105 M-1 s-1) and isobutyl 4-nitrophenyl methylphosphonate (kcat/Km = 1.1 × 104 M-1 s-1). The (SP)-enantiomer of isobutyl 4-nitrophenyl methylphosphonate was hydrolyzed 10 times faster than the less toxic (RP)-enantiomer. The high inherent catalytic activity of Rsp3690 for the hydrolysis of the toxic enantiomer of methylphosphonate esters make this enzyme an attractive target for directed evolution investigations.
Selective reduction of aromatic azides in solution/solid-phase and resin cleavage by employing BF3·OEt2/EtSH. Preparation of DC-81
Kamal, Ahmed,Shankaraiah,Reddy, K. Laxma,Devaiah
, p. 4253 - 4257 (2006)
An efficient method for the reduction of aromatic azides in both solution and solid-phase has been developed by employing BF3·OEt2/EtSH. This report also describes resin cleavage employing this reagent system. Further, this protocol has been utilized for the solution as well as the solid-phase synthesis of pyrrolo[2,1-c][1,4]benzodiazepines, including the naturally occurring antibiotic DC-81 and fused [2,1-b]quinazolinones.
Nickel catalysis for hydrogenation of p-dinitrobenzene to p-phenylenediamine
Shuvalova,Kirichenko,Kustov
, p. 34 - 38 (2017)
The activity of supported nickel catalysts (5–20% Ni) in the hydrogenation of p-dinitrobenzene to p-phenylenediamine was investigated. The catalysts were obtained by ureainduced precipitation. Activated carbon, alumina, titania, and silica gel were evaluated as supports. The most active catalysts, 5%Ni/TiO2 and 20%Ni/SiO2, provided 50–54% yields of p-phenylenediamine at complete dinitrobenzene conversion.
β-Sultams - A novel class of serine protease inhibitors
Beardsell,Hinchliffe,Wood,Wilmouth,Schofield,Page
, p. 497 - 498 (2001)
N-Benzoyl β-sultam is an irreversible inactivator of elastase by sulfonation of the active site serine.
Purification and characterization of an N-terminal acidic amino acid-specific aminopeptidase from soybean cotyledons (glycine max)
Asano, Minao,Nakamura, Nami,Kawai, Misako,Miwa, Tetsuya,Nio, Noriki
, p. 113 - 118 (2010)
A novel enzyme that catalyzes the efficient hydrolysis of Glu-Glu was isolated from soybean cotyledons by ammonium sulfate fractionation and successive column chromatographies of Q-sepharose, Phenyl sepharose, and Superdex 200. The apparent molecular mass of this enzyme was found to be 56kDa and 510 kDa by SDS-polyacrylamide gel electrophoresis and Superdex 200 HR 10/30 column chromatography respectively. The enzyme had high activity against Glu-/7-nitroanilide (/NA) and Asp-pNA, whereas Leu-pNA, Phe-pNA, Ala-/;NA, and Pro-pNA were not hydrolyzed. The synthetic dipeptides Glu-Xxx and Asp-Xxx were hydrolyzed, but Xxx-Glu was not. The digestion of a Glu-rich oligopep-tide, chromogranin A (Glu-Glu-Glu-Glu-Glu-Met-Ala-Val-Val-Pro-Gln-Gly- Leu-Phe-Arg-Gly-NH2) using this purified enzyme was also investigated. Glutamic acid residues were cleaved one by one from the N-terminus. These observations indicate that the enzyme removes glutamyl or aspartyl residues from N-terminal acidic amino acid-containing peptides. It is thought that it was an N-terminal acidic amino acid-specific aminopeptidase from a plant.