14199-15-6Relevant articles and documents
Fe(III)-Catalyzed Aromatic Hydroxylation with H2O2 in the Presence of a Variety of Electron-Transfer Agents
Tamagaki, Seizo,Sasaki, Masaaki,Tagaki, Waichiro
, p. 153 - 158 (1989)
Electron-transfer agents such as N,N,N',N'-tetramethylphenylenediamine (TMPD), ferrocenes, and phenothiazines have been found to mediate the hydroxylation of benzene with H2O2 in the presence of Fe3+.Of these, TMPD catalyst is the most effective to provide phenol in 80percent or better yield based on added H2O2 under the optimized conditions.A general mechanism, involving the rate-determining reduction of Fe3+ to Fe2+ with such mediators, is suggested.
Synthesis and characterization of a novel Mn(III)-(γ-diketone) complex with catalytic and antifungal activity
Dubey, Priti,Yadava, Sudha
, p. 3392 - 3404 (2018)
A novel Mn(III) complex with γ-diketone having general formula [Mn(hdo)3], where hdo = hexane-2,5-dione ligand, has been synthesized and characterized using UV–vis, FT-IR, ESI-mass and EPR spectra, elemental analysis, powder X-ray diffraction, SEM, and magnetic susceptibility measurements. The X-ray diffraction studies reveal that it has monoclinic lattice system with C2/C space group and the unit cell dimensions are a = 9.92245 ?, b = 10.50696 ?, and c = 9.80835 ?. The particle size of this complex has been found to be 32.1 nm. The complex was evaluated for its antifungal activity against Aspergillus flavus, Aspergillus niger, and Aspergillus terreus fungal species. The results indicate that the minimum inhibitory concentration of the synthesized complex was 8 ppm for A. niger while for A. flavus and A. terreus it was 6 ppm. β-Diketone Mn(III) complexes inhibit the fungal growth only partially. This communication is the first report of transformation of a keto-group to an ester group catalyzed by a metal complex.
Identification and Profiling of a Novel Diazaspiro[3.4]octane Chemical Series Active against Multiple Stages of the Human Malaria Parasite Plasmodium falciparum and Optimization Efforts
Le Manach, Claire,Dam, Jean,Woodland, John G.,Kaur, Gurminder,Khonde, Lutete P.,Brunschwig, Christel,Njoroge, Mathew,Wicht, Kathryn J.,Horatscheck, André,Paquet, Tanya,Boyle, Grant A.,Gibhard, Liezl,Taylor, Dale,Lawrence, Nina,Yeo, Tomas,Mok, Sachel,Eastman, Richard T.,Dorjsuren, Dorjbal,Talley, Daniel C.,Guo, Hui,Simeonov, Anton,Reader, Janette,Van Der Watt, Mari?tte,Erlank, Erica,Venter, Nelius,Zawada, Jacek W.,Aswat, Ayesha,Nardini, Luisa,Coetzer, Theresa L.,Lauterbach, Sonja B.,Bezuidenhout, Belinda C.,Theron, Anjo,Mancama, Dalu,Koekemoer, Lizette L.,Birkholtz, Lyn-Marie,Wittlin, Sergio,Delves, Michael,Ottilie, Sabine,Winzeler, Elizabeth A.,Smith, Dennis,Fidock, David A.,Street, Leslie J.,Basarab, Gregory S.,Duffy, James,Chibale, Kelly
supporting information, p. 2291 - 2309 (2021/03/01)
A novel diazaspiro[3.4]octane series was identified from a Plasmodium falciparum whole-cell high-throughput screening campaign. Hits displayed activity against multiple stages of the parasite lifecycle, which together with a novel sp3-rich scaffold provided an attractive starting point for a hit-to-lead medicinal chemistry optimization and biological profiling program. Structure-activity-relationship studies led to the identification of compounds that showed low nanomolar asexual blood-stage activity (50 nM) together with strong gametocyte sterilizing properties that translated to transmission-blocking activity in the standard membrane feeding assay. Mechanistic studies through resistance selection with one of the analogues followed by whole-genome sequencing implicated the P. falciparum cyclic amine resistance locus in the mode of resistance.
Carboxylic Acid Reductase Can Catalyze Ester Synthesis in Aqueous Environments
Pongpamorn, Pornkanok,Kiattisewee, Cholpisit,Kittipanukul, Narongyot,Jaroensuk, Juthamas,Trisrivirat, Duangthip,Maenpuen, Somchart,Chaiyen, Pimchai
supporting information, p. 5749 - 5753 (2021/02/01)
Most of the well-known enzymes catalyzing esterification require the minimization of water or activated substrates for activity. This work reports a new reaction catalyzed by carboxylic acid reductase (CAR), an enzyme known to transform a broad spectrum of carboxylic acids into aldehydes, with the use of ATP, Mg2+, and NADPH as co-substrates. When NADPH was replaced by a nucleophilic alcohol, CAR from Mycobacterium marinum can catalyze esterification under aqueous conditions at room temperature. Addition of imidazole, especially at pH 10.0, significantly enhanced ester production. In comparison to other esterification enzymes such as acyltransferase and lipase, CAR gave higher esterification yields in direct esterification under aqueous conditions. The scalability of CAR catalyzed esterification was demonstrated for the synthesis of cinoxate, an active ingredient in sunscreen. The CAR esterification offers a new method for green esterification under high water content conditions.
A Novel Synthesis of Pimavanserin: A Selective Serotonin 5-HT2A Receptor Inverse Agonist
Hu, Kun,Ren, Jie,Wu, Dongdong,Xie, Yuxuan,Zhang, Meiju
, (2020/01/31)
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