7418-33-9Relevant articles and documents
Regioselective nitration of anilines with Fe(NO3)3·9H2O as a promoter and a nitro source
Gao, Yang,Mao, Yuanyou,Zhang, Biwei,Zhan, Yingying,Huo, Yanping
supporting information, p. 3881 - 3884 (2018/06/08)
An efficient Fe(NO3)3·9H2O promoted ortho-nitration reaction of aniline derivatives has been developed. This reaction may go through a nitrogen dioxide radical (NO2) intermediate, which is generated by the thermal decomposition of iron(iii) nitrate. The practicality of the present method using nontoxic and inexpensive iron reagents has been shown by the broad substrate scope and applications.
A direct, regioselective palladium-catalyzed synthesis of N-substituted benzimidazoles and imidazopyridines
Alonso, Jorge,Halland, Nis,Nazare, Marc,R'Kyek, Omar,Urmann, Matthias,Lindenschmidt, Andreas
supporting information; experimental part, p. 234 - 237 (2011/03/20)
Unsymmetric, N-substituted benzimidazoles and imidazopyridines can be prepared directly from 2-halonitroarenes and amides through Pd(TFA) 2/(R)-BINAP-catalyzed cross-coupling and subsequent reductive aminocyclization. This sequence can be conducted by a one-pot procedure. The method is versatile and allows the straightforward, regioselective preparation of these important nitrogen heterocycles. Unsymmetrical, N-substituted benzimidazoles can be prepared directly from 2-halonitroarenes and amides through Pd(TFA)2/(R)-BINAP-catalyzed cross-coupling and subsequent reductive aminocyclization.This sequence can be conducted by a one-pot procedure. The method is versatile and allows the straightforward, regioselective preparation of these important nitrogen heterocycles. Copyright
On the active site for hydrolysis of aryl amides and choline esters by human cholinesterases
Darvesh, Sultan,McDonald, Robert S.,Darvesh, Katherine V.,Mataija, Diane,Mothana, Sam,Cook, Holly,Carneiro, Karina M.,Richard, Nicole,Walsh, Ryan,Martin, Earl
, p. 4586 - 4599 (2007/10/03)
Cholinesterases, in addition to their well-known esterase action, also show an aryl acylamidase (AAA) activity whereby they catalyze the hydrolysis of amides of certain aromatic amines. The biological function of this catalysis is not known. Furthermore, it is not known whether the esterase catalytic site is involved in the AAA activity of cholinesterases. It has been speculated that the AAA activity, especially that of butyrylcholinesterase (BuChE), may be important in the development of the nervous system and in pathological processes such as formation of neuritic plaques in Alzheimer's disease (AD). The substrate generally used to study the AAA activity of cholinesterases is N-(2-nitrophenyl)acetamide. However, use of this substrate requires high concentrations of enzyme and substrate, and prolonged periods of incubation at elevated temperature. As a consequence, difficulties in performing kinetic analysis of AAA activity associated with cholinesterases have hampered understanding this activity. Because of its potential biological importance, we sought to develop a more efficient and specific substrate for use in studying the AAA activity associated with BuChE, and for exploring the catalytic site for this hydrolysis. Here, we describe the structure-activity relationships for hydrolysis of anilides by cholinesterases. These studies led to a substrate, N-(2-nitrophenyl)trifluoroacetamide, that was hydrolyzed several orders of magnitude faster than N-(2-nitrophenyl)acetamide by cholinesterases. Also, larger N-(2-nitrophenyl)alkylamides were found to be more rapidly hydrolyzed by BuChE than N-(2-nitrophenyl)acetamide and, in addition, were more specific for hydrolysis by BuChE. Thus, N-(2-nitrophenyl)alkylamides with six to eight carbon atoms in the acyl group represent suitable specific substrates to investigate further the function of the AAA activity of BuChE. Based on the substrate structure-activity relationships and kinetic studies, the hydrolysis of anilides and esters of choline appears to utilize the same catalytic site in BuChE.
