• Bulletin of the Korean Chemical Society
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• v.34 no.10
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• pp.2989-2994
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• 2013

The solvolysis rate constants of 3,4- (1) and 3,5-dimethoxybenzoyl (2) chlorides were measured in various pure and binary solvents at $25.0^{\circ}C$, and studied by application of the extended Grunwald-Winstein (G-W) equation, kinetic solvent isotope effect in methanolysis and activation parameters. The solvolysis of 1 was interpreted as the unimolecular pathway due to a predominant resonance effect from para-methoxy substituent like 4-methoxybenzoyl chloride (3), while that of 2 was evaluated as the dual mechanism, with unimolecular or bimolecular reaction pathway according to the character of solvent systems (high electrophilic/nucleophilic) chosen, caused by the inductive effect by two meta-methoxy substituents, no resonance one. In the solvolyses of 1 and 2 with two $-OCH_3$ groups, the resonance effect of para-methoxy substituent is more important to decide the mechanism than the inductive effect with other corresponding evidences.

• Bulletin of the Korean Chemical Society
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• v.34 no.4
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• pp.1096-1100
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• 2013

The kinetic studies on the reactions of O-methyl (1), O-propyl (3) and O-isopropyl (4) phenyl phosphonochloridothioates with substituted anilines and deuterated anilines have been carried out in acetonitrile at $55.0^{\circ}C$. A concerted $S_N2$ mechanism is proposed for the anilinolyses of 1, 3 and 4. The anilinolysis rates of the phosphonochloridothioates are predominantly dependent upon the steric effects over the inductive effects of the two ligands. The deuterium kinetic isotope effects (DKIEs; $k_H/k_D$) are primary normal with 1 and 3, while secondary inverse with 4. Primary normal and secondary inverse DKIEs are rationalized by frontside and backside nucleophilic attack transition state, respectively. The DKIEs of the phosphonochloridothioates do not have any consistent correlations with the two ligands.

• Archives of Pharmacal Research
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• v.22 no.1
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• pp.13-17
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• 1999

The kinetic constants and the reaction mechanism of the K228G mutant horse liver alcohol dehyrogenase isoenzyme E (HLADH-E) were compared to the wild-type enzyme. All the Km and Ki constants of the mutant enzyme for NAD+, ethanol, acetaldehyde and NADH were larger than those of the wild-type enzyme. The dissociation constants for the NADH and $NAD^{+}$ (Kiq and Kia) were greatly increased by 130-and 460-fold, respectively. The product inhibition patterns suggested that the reaction mechanism of the mutant enzyme was changed to Random Bi Bi. These results could attribute to the increase in the dissociation rate of coenzyme with the substitution at Lys-228 residue.

• Bulletin of the Korean Chemical Society
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• v.32 no.11
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• pp.4095-4098
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• 2011

• Journal of the Korean Society of Industry Convergence
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• v.8 no.3
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• pp.155-160
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• 2005

Kinetic studies were carried out for aquation of carbonatobis(ethylenediamine)cobalt(III) complexes in [H+] aqueous solution by UV/VIS-spectrophotometry. The rate law that in deduced from rate data is $rate=k_H{^+}[H^+]^{1.4}$ {$[Co(en)_2(CO_3)]^+$}1.0 where $k_H{^+}$ is the rate constant considering acidic catalyst, $H^+$ ion whose value is $0.241l{\cdot}mol^{-1}{\cdot}sec^{-1}$. The values of activation parameters Ea, ${\Delta}H^{\ast}$ and ${\Delta}S^{\ast}$ were $15.33Kcal{\cdot}mol^{-1}$, $14.52Kcal{\cdot}mol^{-1}$ and -57.49 e.u. respectively. On the basis of kinetic data and the observed activation parameters, we have proposed the mechanism that proceeds with two step protonations. The rate equation derived from the proposed mechanism has been in agreement with the observed rate equation. It has been seen that our modified mechanism for Harris's proton freequilibrium one prefer to the his concerted mechanism, and more the last product substitute $H_2O$ for $OH^-$ the Harris's mechanism in the acidity range 2 < pH < 5.

• Bulletin of the Korean Chemical Society
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• v.23 no.9
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• pp.1347-1350
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• 2002

• Bulletin of the Korean Chemical Society
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• v.32 no.10
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• pp.3799-3801
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• 2011

• Bulletin of the Korean Chemical Society
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• v.27 no.1
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• pp.143-146
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• 2006

• Journal of Powder Materials
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• v.24 no.1
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• pp.6-10
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• 2017

This study investigates the main growth mechanism of InP during InP/ZnS reaction of quantum dots (QDs). The size of the InP core, considering a synthesis time of 1-30 min, increased from the initial 2.56 nm to 3.97 nm. As a result of applying the proposed particle growth model, the migration mechanism, with time index 7, was found to be the main reaction. In addition, after the removal of unreacted In and P precursors from bath, further InP growth (of up to 4.19 nm (5%)), was observed when ZnS was added. The full width at half maximum (FWHM) of the synthesized InP/ZnS quantum dots was found to be relatively uniform, measuring about 59 nm. However, kinetic growth mechanism provides limited information for InP / ZnS core shell QDs, because the surface state of InP changes with reaction time. Further study is necessary, in order to clearly determine the kinetic growth mechanism of InP / ZnS core shell QDs.

• Bulletin of the Korean Chemical Society
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• v.24 no.1
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• pp.65-69
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• 2003

The kinetic and chemical mechanisms of AChE-catalyzed hydrolysis of short-chain thiocholine esters are relatively well documented. Up to propanoylthiocholine (PrTCh) the chemical mechanism is general acid-base catalysis by the active site catalytic triad. The chemical mechanism for the enzyme-catalyzed butyrylthiocholine(BuTCh) hydrolysis shifts to a parallel mechanism in which general base catalysis by E199 of direct water attack to the carbonyl carbon of the substrate. [Selwood, T., et al. J. Am. Chem. Soc. 1993, 115, 10477- 10482] The long chain thiocholine esters such as hexanoylthiocholine (HexTCh), heptanoylthiocholine (HepTCh), and octanoylthiocholine (OcTCh) are hydrolyzed by electric eel acetylcholinesterase (AChE). The kinetic parameters are determined to show that these compounds have a lower Michaelis constant than BuTCh and the pH-rate profile showed that the mechanism is similar to that of BuTCh hydrolysis. The solvent isotope effect and proton inventory of AChE-catalyzed hydrolysis of HexTCh showed that one proton transfer is involved in the transition state of the acylation stage. The relationship between the dipole moment and the Michaelis constant of the long chain thiocholine esters showed that the dipole moment is the most important factor for the binding of a substrate to the enzyme active site.