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Abstract
The reduction of horse heart ferricytochrome c in neutral and slightly alkaline solutions follows biphasic kinetics. The obtained results are consistent with the existence of two conformational forms of ferricytochrome c, cyt c and cyt c ∗. The conversion of cyt c to cyt c ∗ occurs by deprotonation (pK∼7), followed by a slow conformational change in the protein structure.
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