[Conformation and reduction-oxidation properties of cytochrome c incorporated into reversed micelles of a surfactant in an organic solvent].

Changes observed in CD- and absorption spectra of cytochrome c solubilized in reversed micelles AOT showed significant structural transformations of protein in the region of the active centre and particularly revealed a replacement of the sixth ligand of heme iron. These changes also affected the redox properties of cytochrome c.