394-41-2Relevant articles and documents
A 4 - amino -3 - fluoro phenol high efficient synthesis method (by machine translation)
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Page/Page column 4; 5; 6; 7, (2019/01/05)
The invention discloses a 4 - amino - 3 - fluoro phenol high efficient synthesis method, specifically comprises the following steps: first preparing porous polystyrene micro-ball, and then added to the hydrolysate of titanium tetrachloride, the reaction is carried out under certain conditions to make the supported catalyst, finally a pair of nitro phenol as raw materials to make the 3 - fluoro - - 4 nitro phenol, then in the above prepared under the catalysis of the supported catalyst, dropping the sodium borohydride solution reaction, to obtain the target product. The method is simple in operation, the equipment requirement is low, the yield is high. (by machine translation)
4-amino-3-fluorophenol and synthesizing method thereof
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Paragraph 0020; 0023, (2016/10/10)
The invention discloses 4-amino-3-fluorophenol and a synthesizing method thereof.The synthesizing method comprises the steps that fluoroaniline serves as a raw material, a diazo-reaction is carried out first, then a fluorine resolving reaction is carried out, and a white diazonium salt solid is obtained; then, the white diazonium salt solid is subjected to a hydrolysis reaction, and 3-fluorophenol is obtained; 3-fluorophenol is then subjected to a nitration reaction, and 3-fluorine-4-nitrophenol is obtained; then, obtained 3-fluorine-4-nitrophenol is reduced, and 4-amino-3-fluorophenol is obtained.According to 4-amino-3-fluorophenol and the synthesizing method thereof, ionic liquid serves as a reaction solvent, the volatility is low, environment is easily protected, and no harm is caused to the human body; in the reaction of reducing nitro groups into amino groups, the microwave heating mode is adopted, so that the reaction efficiency is greatly improved, and the product yield is increased.
Probing synergy between two catalytic strategies in the glycoside hydrolase O-GlcNAcase using multiple linear free energy relationships
Greig, Ian R.,Macauley, Matthew S.,Williams, Ian H.,Vocadlo, David J.
supporting information; experimental part, p. 13415 - 13422 (2010/01/16)
Human O-GlcNAcase plays an important role in regulating the post-translational modification of serine and threonine residues with β-O-linked N-acetylglucosamine monosaccharide unit (O-GlcNAc). The mechanism of O-GlcNAcase involves nucleophilic participation of the 2-acetamido group of the substrate to displace a glycosidically linked leaving group. The tolerance of this enzyme for variation in substrate structure has enabled us to characterize O-GlcNAcase transition states using several series of substrates to generate multiple simultaneous free-energy relationships. Patterns revealing changes in mechanism, transition state, and rate-determining step upon concomitant variation of both nucleophilic strength and leaving group abilities are observed. The observed changes in mechanism reflect the roles played by the enzymic general acid and the catalytic nucleophile. Significantly, these results illustrate how the enzyme synergistically harnesses both modes of catalysis; a feature that eludes many small molecule models of catalysis. These studies also suggest the kinetic significance of an oxocarbenium ion intermediate in the O-GlcNAcase-catalyzed hydrolysis of glucosaminides, probing the limits of what may be learned using nonatomistic investigations of enzymic transition-state structure and offering general insights into how the superfamily of retaining glycoside hydrolases act as efficient catalysts.
