84571-26-6Relevant articles and documents
Design, synthesis, and enzymatic characterization of quinazoline-based CYP1A2 inhibitors
Botello, Jordy F.,Corral, Pedro A.,Xing, Chengguo
supporting information, (2019/12/11)
Cytochrome P450 isozyme 1A2 (CYP1A2) is one main xenobiotic metabolizing enzyme in humans. It has been associated with the bioactivation of procarcinogens, including 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK), a tobacco specific and potent pulmo
Ru(II)-arene complexes with N-substituted 3,4-dihydroquinazoline ligands and catalytic activity for transfer hydrogenation reaction
Mercan, Deniz,?etinkaya, Engin,?ahin, Ertan
supporting information, p. 74 - 81 (2013/07/19)
In this study, N-coordinated 3,4-dihydroquinazoline ruthenium(II) complexes were synthesized by the cleavage reaction of [RuCl2(p-cymene)] 2 with N-substituted 3,4-dihydroquinazolines. In addition, the X-ray crystal structure of 2,4,6-trimethylbenzyl substituted 3,4-dihydroquinazoline Ru(II) complex (1a) is reported. Furthermore, the resulting piano-stool complexes were evaluated as transfer hydrogenation catalysts for reduction of acetophenone in the presence of 2-propanol and KOH at 82°C. All the complexes showed good to excellent performance after 1 h in the conversion of acetophenone to alcohol and the reaction rate was found to be sensitive to changes on the N-substituent. Additionally, the most active catalyst 1a was used in transfer hydrogenation of different ketones to investigate the effect of substituents on ketones.
