Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide.
The oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, Thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. Ferrohexacyanide was used as reductant. (Formula: see text.) Thermodynamic and activation parameters of the reaction obtained for both cytochromes were compared with each other. The results of this showed that (1) the redox potential of cytochrome c-552, + 0.19 V, is markedly less than that of horse heart cytochrome c. (2) deltaHox of cytochrome c-552 is considerably lower than that of horse heart cytochrome c. (3) deltaSox and deltaSred of cytochrome c-552 are more negative than those of horse heart cytochrome c. (4) kred of cytochrome c-552 is much lower than that of horse heart cytochrome c at room temperature.
D000818:Animals; D001419:Bacteria; D003574:Cytochrome c Group; D005295:Ferrocyanides; D006736:Horses; D007700:Kinetics; D008433:Mathematics; D010084:Oxidation-Reduction; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D013816:Thermodynamics
D003574:Cytochrome c Group; D005295:Ferrocyanides