scholarly journals The Mechanism of the Reaction of (Arylthio)trimethylgermanes with Benzyl Bromides Giving Aryl Benzyl Sulfides. A Kinetic Study

1987 ◽  
Vol 60 (11) ◽  
pp. 4061-4065 ◽  
Author(s):  
Seizi Kozuka ◽  
Shoji Tamura ◽  
Satoshi Ishibashi ◽  
Sadamu Ohya ◽  
Waichiro Tagaki
1976 ◽  
Vol 54 (5) ◽  
pp. 706-710 ◽  
Author(s):  
James P. K. Tong ◽  
Cooper H. Langford

The rates of nickel(II)–murexide complex formation were studied in dimethylsulfoxide/nitromethane mixed solvents at 25 °C with the latter being an "inert" solvent, to elucidate the mechanism of the reaction. Results do not fit in detail with a D mechanism and the five-coordinated intermediate interpretation. Id mechanisms are able to explain the observations with and without invoking a nitromethane-containing intermediate, Ni(DMSO)5NM2+. Both mechanisms were tested with the aid of nmr data on solvation (second coordinate sphere nitromethane population). Ligand solvation unavoidably plays a major role in the determination of the encounter as well as the complex formation equilibrium. The simplest mechanism assumes an Id process in which the probability of encounter between Ni(DMSO)62+ and murexide ion is quite sensitive to solvent composition.


2007 ◽  
Vol 3 (3) ◽  
pp. 222-228
Author(s):  
Lugard Ukiwe ◽  
C.I.A. Nwoko ◽  
Okere-Chijioke M

An investigation into the kinetics of two inorganic coagulant namely: aluminum sulphate octadecahydrate (Al2(SO4)3.18H2O) an ammonium aluminum sulphate dodecahydrate (NH4Al(SO4)2.12H2O) was studied to determine the effect of certain kinetic parameters on coagulation performance of the above mentioned coagulants. Results of analysis obtained revealed that the rate constant (k) for Al2(SO4)3.18H2O was 5.727s-1, while that for NH4Al(SO4)2.12H2O was 2.282s-1. However, the order of the reaction (xn) of Al2(SO4)3.18H2O and NH4Al(SO4)2.12H2O with the wastewater was 1.0 and 1.0, respectively, indicating that both reactions were first order. Considering the mechanism of the reaction, the general trend observed indicated that the Al2(SO4)3.18H2O reaction was thrice as fast as the NH4Al(SO4)2.12H2O reaction. This fact together with the larger value of k for Al2(SO4)3.18H2O obtained in the experiment lend credence to the widely held believe that Al2(SO4)3.18H2O is a more effective coagulant than NH4Al(SO4)2.12H2O in wastewater treatment.


1966 ◽  
Vol 44 (23) ◽  
pp. 2793-2803 ◽  
Author(s):  
A. William Johnson ◽  
Simon C. K. Wong

The pKa values of two series of iminophosphoranes, N-(substituted phenyl)-iminotriphenylphosphoranes (VI) and N-phenyliminotri-(substituted phenyl)-phosphoranes (VII), have been correlated with σ0 and σ, respectively, giving ρ values of +3.5 and +9.3. A kinetic study of the reaction of VI and VII with benzaldehydes indicates that a betaine intermediate (V) is involved. The rate-limiting step of the reaction changes, the result of a delicate balance between the nucleophilicity of the nitrogen atom and the electrophilicity of the phosphorus atom. The involvement of dπ–pπ bonding is indicated.


2016 ◽  
Vol 1 (16) ◽  
pp. 5141-5151 ◽  
Author(s):  
Yota Suzuki ◽  
Mika Shimizu ◽  
Takuya Okamoto ◽  
Tomoaki Sugaya ◽  
Satoshi Iwatsuki ◽  
...  

2008 ◽  
Vol 105 (12) ◽  
pp. 601-608
Author(s):  
Seung Min Han ◽  
Dong Joon Min ◽  
Joo Hyun Park ◽  
Jung Ho Park ◽  
Jong Min Park
Keyword(s):  

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev

SummaryIt was found that the effect of heparin on the amidase activity of urokinase (E C 3.4.21.31), plasmin (E C 3.4.21.7) and trypsin (E C 3.4.21.4) depended on the substrate used. No effect of heparin on the amidase activity of urokinase and trypsin was observed when Pyro Glu-Gly-Arg-p-nitroanilide (S-2444) and α-N-acetyl-L-lysine-p-nitroanilide (ALNA) were used as substrates. Heparin acted as a uncompetitive inhibitor of trypsin (Ki = 1.2×10-6 M), plasmin (Ki = 4.9×10-6 M) and urokinase (Ki = l.0×10-7 M) when Bz-Phe-Val-Arg-p-nitroanilide (S-2160), H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and plasminogen, respectively, were used as substrates. These results, as well as the data obtained by studying the effect of the simultaneous presence of heparin and competitive inhibitors suggest that although heparin is not bound at the active center of these enzymes, it may influence the effectivity of catalysis.


1981 ◽  
Vol 31 (1) ◽  
pp. 388-394 ◽  
Author(s):  
Mahmoud El-Sawi ◽  
Antonio Iannibello ◽  
Fernando Morelli ◽  
Ganfranco Gatalano ◽  
Francesco Intrieri ◽  
...  
Keyword(s):  

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