5208-87-7Relevant articles and documents
Metabolism of 7-ethoxycoumarin, safrole, flavanone and hydroxyflavanone by cytochrome P450 2A6 variants
Uno, Tomohide,Obe, Yuichiro,Ogura, Chika,Goto, Tatsushi,Yamamoto, Kohei,Nakamura, Masahiko,Kanamaru, Kengo,Yamagata, Hiroshi,Imaishi, Hiromasa
, p. 87 - 97 (2013)
CYP 2A6 is a human enzyme that metabolizes many xenobiotics including coumarin, indole, nicotine and carcinogenic nitrosamines. The gene for CYP2A6 is polymorphic. There are few data available to clarify the relationship between P450 genetic variants and the metabolism of materials in food. The CYP 2A6 wild-type protein and 13 mutants (CYP2A6.1, CYP2A6.2, CYP2A6.5, CYP2A6.6, CYP2A6.7, CYP2A6.8, CYP2A6.11, CYP2A6.15, CYP2A6.16, CYP2A6.17, CYP2A6.18, CYP2A6.21, CYP2A6.23 and CYP2A6.25) were co-expressed with NADPH-cytochrome P450 reductase in E. coli. The hydroxylase activities toward 7-ethoxycoumarin, coumarin, safrole, flavanone and hydroxyflavanone were examined. Ten types of CYP2A6 variants except for CYP2A6.2, CYP2A6.5 and CYP2A6.6 showed Soret peaks (450 nm) typical of P450 in the reduced CO-difference spectra and had 7-ethoxycoumarin O-deethylase activities. CYP2A6.15 and CYP2A6.18 showed higher activities for safrole 1′-hydroxylation than CYP2A6.1. CYP2A6.25 and CYP2A6.7 had lower safrole 1′-hydroxylase activities. CYP2A6.7 had lower flavanone 6- and 2′-hydroxylase activities, whereas CYP2A6.25 had higher 6-hydroxylase activity and lower 2′-hydroxylase activity. Hydroxyflavanone was metabolized by CYP2A6.25, but was not metabolized by wild-type CYP2A6.1. These results indicate that CYP2A6.25 possessed new substrate specificity toward flavonoids. Copyright 2012 John Wiley & Sons, Ltd. Copyright
Allylic and Allenylic Dearomatization of Indoles Promoted by Graphene Oxide by Covalent Grafting Activation Mode
Lombardi, Lorenzo,Bellini, Daniele,Bottoni, Andrea,Calvaresi, Matteo,Monari, Magda,Kovtun, Alessandro,Palermo, Vincenzo,Melucci, Manuela,Bandini, Marco
supporting information, p. 10427 - 10432 (2020/07/24)
The site-selective allylative and allenylative dearomatization of indoles with alcohols was performed under carbocatalytic regime in the presence of graphene oxide (GO, 10 wt percent loading) as the promoter. Metal-free conditions, absence of stoichiometric additive, environmentally friendly conditions (H2O/CH3CN, 55 °C, 6 h), broad substrate scope (33 examples, yield up to 92 percent) and excellent site- and stereoselectivity characterize the present methodology. Moreover, a covalent activation model exerted by GO functionalities was corroborated by spectroscopic, experimental and computational evidences. Recovering and regeneration of the GO catalyst through simple acidic treatment was also documented.
Chemoselective α,β-Dehydrogenation of Saturated Amides
Teskey, Christopher J.,Adler, Pauline,Gon?alves, Carlos R.,Maulide, Nuno
supporting information, p. 447 - 451 (2019/01/04)
We report a method for the selective α,β-dehydrogenation of amides in the presence of other carbonyl moieties under mild conditions. Our strategy relies on electrophilic activation coupled to in situ selective selenium-mediated dehydrogenation. The α,β-unsaturated products were obtained in moderate to excellent yields, and their synthetic versatility was demonstrated by a range of transformations. Mechanistic experiments suggest formation of an electrophilic SeIV species.