Kinetics of electron transfer between mitochondrial cytochrome c and iron hexacyanides.
The reduction of horse and Candida krusei cytochromes c by ferrocyanide has been studied by 1H NMR spectroscopy and the reaction found to involve a precursor complex of ferrocyanide bound to ferricytochrome c (pH* 7.4, 2H2O, I = 0.12, and 25 degrees C). The electron transfer rate constants for the reduction of the two ferricytochromes by associated ferrocyanide were found to be the same at 780 +/- 80 sec-1 but the association constants for binding of ferrocyanide to ferricytochrome c were significantly different: horse, 90 +/- 20 M-1 and Candida, 285 +/- 30 M-1. The different association constants partly accounts for the previously observed reactivity difference between horse and Candida cytochromes c. Comparison of the NMR data with data obtained by other kinetic methods has allowed the electron transfer rate constant for the oxidation of ferrocytochrome c by associated ferricyanide to be determined. This was found to be 4.6 +/- 1 X 10(4) sec-1.
D000818:Animals; D002175:Candida / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism*; D004579:Electron Transport; D005292:Ferricyanides; D006736:Horses; D007700:Kinetics; D008433:Mathematics; D008928:Mitochondria / Q000378:metabolism*
D003574:Cytochrome c Group; D005292:Ferricyanides; C007931:hexacyanoferrate III