A kinetic study of concomitant addition and deprotonation reactions of ferrocenyl-stabilised carbocations in aqueous acetonitrile and of the reverse reactions

Author(s):  
Clifford A. Bunton ◽  
Nelson Carrasco ◽  
Norman Cully ◽  
William E. Watts
2016 ◽  
Vol 15 (2) ◽  
pp. 33-44
Author(s):  
John K Adaikalasamy ◽  
Selva A Priya ◽  
Sunaja K R Devi

Iron(III)-bipyridine complex was prepared andcharacterized by UV-Visible spectrophotometer. Kineticstudy was carried out by using this iron(III)-bipyridinewith thiodipropionic acid in aqueous acetonitrile solution.The reaction was optimized by studying the effect onsubstrate, solvent, oxidant, acidity and temperature. Firstorder, second order rate constants and activationparameters were calculated. The above reaction wasfound to be second order and proceeded through electrontransfer from thiodipropionic acid to iron(III)-bipyridinecomplex. The product was characterized and confirmedby IR and NMR spectroscopy.Keywords: Thiodipropionic acid, Iron(III)-bipyridine complex,kinetic study of Iron(III)-bipyridyl complexes.


1970 ◽  
Vol 48 (17) ◽  
pp. 2718-2721 ◽  
Author(s):  
Richard L. Reeves

A kinetic study of the electron-transfer reaction between a model azobenzene and dihydrophenazonium ion-radical and dihydrophenazine was carried out in 0.2 N sulfuric acid in 50 v/v aqueous acetonitrile. The second-order rate constant for the dihydrophenazine is greater than that of the ion-radical by a factor of 104. It is shown that in solutions in which the ion-radical is the predominant species, the principal electron-transfer agent is the dihydrophenazine formed by dismutation of the radical.


2017 ◽  
Vol 49 (8) ◽  
pp. 622-632 ◽  
Author(s):  
Y. Hemanth Sriram ◽  
Touheeth Fatima ◽  
K. C. Rajanna ◽  
M. Satish Kumar ◽  
R. Madhusudan Raju

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):  

Sign in / Sign up

Export Citation Format

Share Document