Abstract
This chapter elaborates about kinetic and equilibrium studies on the autoreduction of horse-heart ferricytochrome c. X-ray crystallographic studies on horse-heart ferricytochrome c have conclusively proved that the heme group lies in a crevice formed by the polypeptide chain with only one of its edges exposed to the solvent, thus confirming the heme in a crevice structure. Horse-heart cytochrome c was prepared as described for bovine-heart cytochrome c and obtained in the monomeric form by molecular sieve chromatography on Sephadex G-75. Ferricytochrome c is spontaneously reduced within the whole pH range from 6.7 to 11.0, i.e., reduced slowly in the absence of any chemical reducing agent. The autoreduction was followed over a period of several hours, i.e., until a steady state of oxidation/reduction was obtained.
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