Mechanism of Hydrolysis of Ethyl Benzimidates in Acidic Solutions

1965 ◽  
Vol 30 (3) ◽  
pp. 699-702 ◽  
Author(s):  
Robert H. DeWolfe ◽  
Frederick B. Augustine
Author(s):  
Vladan J. Anićijević ◽  
Milena Petković ◽  
Igor A Pašti ◽  
Tamara Lazarević-Pašti

Organophosphate pesticides are used in large quantities. However, they exhibit toxic effects on non-target organisms. Dimethoate and its oxo-analog omethoate inhibit acetylcholinesterase and are toxic for mammals. Moreover, they show extreme toxicity for bees. Once in the environment, they undergo chemical transformations and decomposition. We show that dime-thoate and omethoate decompose rapidly in alkaline aqueous solutions (half-lives 5.7 and 0.89 days) but are highly stable in acidic solutions (half-lives 124 and 104 days). These differences are explained using quantum chemical calculations, indicating that a weaker P–S bond in omethoate is more susceptible to hydrolysis, particularly at a high pH. The toxicity of these pesticides solutions decreases over time, indicating that no or very little highly toxic omethoate is formed during hydrolysis. Presented data can be used to predict dimethoate and omethoate concentrations in contaminated water depending on pH. Presented results suggest that alkaline hydrolysis of organophosphates has an advantage over other techniques for their removal since there is no risk of omethoate accumulation and increased toxicity of contaminated water.


1966 ◽  
Vol 5 (11) ◽  
pp. 1943-1946 ◽  
Author(s):  
Franklin H. Fry ◽  
Gordon A. Hamilton ◽  
John Turkevich

1982 ◽  
Vol 35 (7) ◽  
pp. 1357 ◽  
Author(s):  
TJ Broxton

The hydrolysis of 2-acetyloxybenzoic acid in the pH range 6-12 has been studied in the presence of micelles of cetyltrimethylammonium bromide (ctab) and cetylpyridinium chloride (cpc). In the plateau region (pH 6-8) the hydrolysis is inhibited by the presence of micelles, while in the region where the normal BAC2 hydrolysis (pH > 9) occurs the reaction is catalysed by micelles of ctab and cpc. The mechanism of hydrolysis in the plateau region is shown to involve general base catalysis by the adjacent ionized carboxy group both in the presence and absence of micelles. This reaction is inhibited in the presence of micelles because the substrate molecules are solubilized into the micelle and water is less available in this environment than in normal aqueous solution.


2002 ◽  
Vol 57 (11-12) ◽  
pp. 1072-1077 ◽  
Author(s):  
Karel Komers ◽  
Alexandr Čegan ◽  
Marek Link

Kinetics and mechanism of hydrolysis of acetylthiocholine by the enzyme butyrylcholine esterase was studied. The spectrophotometric Ellman’s method and potentiometric pH-stat method were used for continuous determination of the actual concentration of the products thiocholine and acetic acid in the reaction mixture. The validity of the Michaelis-Menten (Briggs-Haldane) equation in the whole course of the reaction under used conditions was proved. The corresponding kinetics parameters (Vm and KM) were calculated from the obtained dependences of concentration of thiocholine or acetic acid vs. time and compared. From this comparison the deciding kinetic role of the step producing thiocholine was derived. The values of initial molar concentration of the enzyme and of the rate constants of the kinetic model were estimated.


Author(s):  
Sergey Varfolomeev ◽  
Bella Grigorenko ◽  
Sofya Lushchekina ◽  
Alexander Nemuchin

The work is devoted to modeling the elementary stages of the hydrolysis reaction in the active site of enzymes belonging to the class of cholinesterases — acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The study allowed to describe at the molecular level the effect of the polymorphic modification of BChE, causing serious physiolog ical consequences. Cholinesterase plays a crucial role in the human body. AChE is one of the key enzymes of the central nervous system, and BChE performs protective functions in the body. According to the results of calculations using the combined method of quantum and molecular mechanics (KM/MM), the mechanism of the hydrolysis of the native acetylcholine substrate in the AChE active center was detailed. For a series of ester substrates, a method for estimation of dependence of the enzyme reactivity on the structure of the substrate has been developed. The mechanism of hydrolysis of the muscle relaxant of succininylcholine BChE and the effect of the Asp70Gly polymorph on it were studied. Using various computer simulation methods, the stability of the enzyme-substrate complex of two enzyme variants with succinylcholine was studied.


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