scholarly journals Horse heart cytochrome c. The oxidation-reduction potential and protein structures.

1979 ◽  
Vol 254 (22) ◽  
pp. 11202-11207
Author(s):  
Y.P. Myer ◽  
A.F. Saturno ◽  
B.C. Verma ◽  
A. Pande
1957 ◽  
Vol 44 (8) ◽  
pp. 535-536 ◽  
Author(s):  
KOITI TITANI ◽  
HISAYUKI ISHIKURA ◽  
SHIGEKI MINAKAMI

Nature ◽  
1956 ◽  
Vol 177 (4521) ◽  
pp. 1180-1181 ◽  
Author(s):  
R. W. HENDERSON ◽  
W. A. RAWLINSON

1991 ◽  
Vol 56 (2) ◽  
pp. 478-490 ◽  
Author(s):  
Joaquin F. Perez-Benito ◽  
Conchita Arias

The reaction between horse-heart cytochrome c and ascorbic acid has been investigated in the pH range 5.5 – 7.1 and at 10.0 – 25.0 °C. The rate shows a first-order dependence on the concentration of cytochrome c, it increases in a non-linear way as the concentration of ascorbic acid increases, it increases markedly with increasing pH and, provided that the ionic strength of the medium is high enough, it fulfills the Arrhenius equation. The apparent activation energy increases as the pH of the solution increases. The results have been explained by means of a mechanism that includes the existence of an equilibrium between two forms (acidic and basic) of oxidized cytochrome c: cyt-H+ -Fe3+ + OH- cyt -Fe3+ + H2O, whose equilibrium constant is (6.7 ± 1.4). 108 at 25.0 °C, the acidic form being more reducible than the basic one. It is suggested that there is a linkage of hydrogenascorbate ion to both forms of cytochrome c previous to the redox reactions. Two possibilities for the oxidant-reductant linkage (binding and adsorption) are discussed in detail.


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