953-01-5Relevant articles and documents
Visible-Light-Promoted Diboron-Mediated Transfer Hydrogenation of Azobenzenes to Hydrazobenzenes
Song, Menghui,Zhou, Hongyan,Wang, Ganggang,Ma, Ben,Jiang, Yajing,Yang, Jingya,Huo, Congde,Wang, Xi-Cun
, p. 4804 - 4811 (2021/04/06)
A visible-light-promoted transfer hydrogenation of azobenzenes has been developed. In the presence of B2pin2 and upon visible-light irradiation, the reactions proceeded smoothly in methanol at ambient temperature. The azobenzenes with diverse functional groups have been reduced to the corresponding hydrazobenzenes with a yield of up to 96%. Preliminary mechanistic studies indicated that the hydrogen atom comes from the solvent and the transformation is achieved through a radical pathway.
Conversion of azobenzenes into N,N′-diarylhydrazines by sodium dithionite
Sydnes, Leiv K.,Elmi, Shire,Heggen, Per,Holmelid, Bjarte,Malthe-S?rensen, Didrik
, p. 1695 - 1698 (2007/12/28)
A number of chloro-, methyl- and methoxy-substituted azobenzenes have been reduced to the corresponding hydrazines by using an aqueous solution of Na 2S2O4. The yield is generally excellent, but two compounds, viz. 4,4-dimethoxyazobenzene and 2,2,4,4,6,6- hexamethylazobenzene, gave no hydrazine at all. Georg Thieme Verlag Stuttgart.
Pyrazolidine-3,5-diones and 5-hydroxy-1H-pyrazol-3(2H)-ones, inhibitors of UDP-N-acetylenolpyruvyl glucosamine reductases
Gilbert, Adam M.,Failli, Amedeo,Shumsky, Jay,Yang, Youjun,Severin, Anatoly,Singh, Guy,Hu, William,Keeney, David,Petersen, Peter J.,Katz, Alan H.
, p. 6027 - 6036 (2007/10/03)
A series of pyrazolidine-3,5-dione and 5-hydroxy-1H-pyrazol-3(2H)-one inhibitors of Escherichia coli UDP-N-acetylenolpyruvyl glucosamine reductase (MurB) has been prepared. The 5-hydroxy-1H-pyrazol-3(2H)-ones show low micromolar IC50 values versus E. coli MurB and submicromolar minimal inhibitory concentrations (MIC) against Staphylococcus aureus GC 1131, Enterococcus faecalis GC 2242, Streptococcus pneumoniae GC 1894, and E. coli GC 4560 imp, a strain with increased outer membrane permeability. None of these compounds show antimicrobial activity against Candida albicans, a marker of eukaryotic toxicity. Moreover, these compounds inhibit peptidoglycan biosynthesis, as assessed by measuring the amount of soluble peptidoglycan produced by Streptococcus epidermidis upon incubation with compounds. A partial least squares projection to latent structures analysis shows that improving MurB potency and MIC values correlate with increasing lipophilicity of the C-4 substituent of the 5-hydroxy-1H-pyrazol-3(2H)-one core. Docking studies using FLO and PharmDock produced several binding orientations for these molecules in the MurB active site.