3229-70-7Relevant articles and documents
The rate of excited-state proton transfer to solvent from trifluoromethylphenols in water
Kaneko, Shigeo,Yoshihara, Toshitada,Tobita, Seiji
, p. 312 - 313 (2009)
The proton-transfer reactions to solvent from electronically excited o-, m-, and p-(trifluoromethyl)phenols (TFOHs) in water have been investigated by picosecond time-resolved fluorescence measurements. The rate constants for the proton dissociation of o-, m-, and p-TFOH are obtained to be 2.2 × 10 9, 8.6 × 108, and 2.5 × 108 s -1, respectively. On the basis of the rate constants, the effects of substituent and deuterium isotope effects on the proton-transfer reactions are revealed. copyright
Kinetics and Mechanism of the Aminolysis of Phenyl Thionoacetate in Aqueous Solution
Castro, Enrique A.,Ibanez, Fernando,Santos, Jose G.,Ureta, Carmen
, p. 4908 - 4912 (1993)
The reactions of a series of secondary alicyclic amines with the title substrate have been subjected to a kinetic study in water at 25 deg C, ionic strength 0.2 M.Pseudo-first-order rate coefficients (kobsd) are found throughout, under amine ex
NEW INSIGHT INTO THE MECHANISMS OF REACTIONS BETWEEN SOME ANIONIC NUCLEOPHILES AND PHENYL ACETATE IN THE GAS PHASE
Kleingeld, Jan C.,Nibbering, Nico M.M.,Grabowski, Joseph J.,DePuy, Charles H.,Fukuda, Elaine K.,McIver, Robert T.
, p. 4755 - 4758 (1982)
Experiments carried out in an ion cyclotron resonance (ICR) drift cell, an ICR trapped ion cell and a flowing afterglow (FA) system show that in the gas phase phenyl acetate reacts with a variety of clustered and unclustered nucleophiles to yield mainly the product ion C6H5O-.
Kinetic Study on Nucleophilic Substitution Reactions of O-Phenyl O-Y-substituted-Phenyl Thionocarbonates with 1,8-Diazabicyclo[5.4.0]undec-7-ene in Acetonitrile
Um, Ik-Hwan,Park, Kyoung-Ho
, p. 1169 - 1173 (2017/09/13)
Second-order rate constants (kN) for nucleophilic substitution reactions of O-phenyl O-Y-substituted-phenyl thionocarbonates (4a–4k) with 1,8-diazabicyclo[5.4.0]undec-7-ene (DBU) in MeCN at 25.0 ± 0.1°C are reported. The reactivity of 4a–4k decreases as basicity of the leaving group increases except O-2,4-dinitrophenyl O-phenyl thionocarbonate (4a), which is less reactive than O-3,4-dinitrophenyl O-phenyl thionocarbonate (4b) although the former possesses 2 pKa units less basic nucleofuge than the latter. The Br?nsted-type plot for the reactions of 4b–4k is linear with βlg = ?0.50, a typical βlg value for reactions reported to proceed through a concerted mechanism. The Hammett plot correlated with σY? constants for the reactions of 4b–4k results in a better linear correlation than that correlated with σYo constants. Besides, the Yukawa-Tsuno plot exhibits an excellent linear correlation with ρY = 2.12, r = 0.68 and R2 = 0.990, indicating that a negative charge develops partially on the O atom of the leaving group in the rate-determining step (RDS). Thus, the reactions have been concluded to proceed through a forced concerted mechanism. Effects of steric hindrance on reactivity and reaction mechanism are also discussed in detail.
Alkaline hydrolysis of Y-substituted phenyl phenyl thionocarbonates: Effect of changing electrophilic center from C=O to C=S on reactivity and mechanism
Kim, Song-I,Park, Hey-Ran,Um, Ik-Hwan
scheme or table, p. 179 - 182 (2011/10/31)
Second-order rate constants (kOH-) have been measured spectrophotometrically for reactions of Y-substituted phenyl phenyl thionocarbonates (4a-i) with OH- in 80 mol % H2O/20 mol % DMSO at 25.0 ± 0.1 °C. The ksu
Structure and mechanism of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway
He, Shu-Mei,Wathier, Matthew,Podzelinska, Kateryna,Wong, Matthew,McSorley, Fern R.,Asfaw, Alemayehu,Hove-Jensen, Bjarne,Jia, Zongchao,Zechel, David L.
experimental part, p. 8603 - 8615 (2012/07/27)
PhnP is a phosphodiesterase that plays an important role within the bacterial carbon-phosphorus lyase (CP-lyase) pathway by recycling a "dead-end" intermediate, 5-phospho-α-d-ribosyl 1,2-cyclic phosphate, that is formed during organophosphonate catabolism
