Solubilisation of ferricytochrome c in methanol using a crown ether: absorption, circular dichroism and EPR spectral properties
Bowyer, J.R.; Odell, B.
Biochemical and Biophysical Research Communications 127(3): 828-835
1985
ISSN/ISBN: 0006-291X PMID: 2985061 Document Number: 264439
Ferricytochrome c is normally insoluble in methanol [MeOH] but its solution is facilitated by complexation with 18-crown-6. Absorption, circular dichroism and EPR spectroscopy indicate that the solubilized protein in MeOH exists in at least 3 conformational states, all different from the native state in neutral aqueous solution. In 2 states, the heme iron (III) is low spin and in one state it is high spin, but it seems likely that all 3 forms are globular. The proportion in the high spin form increases at increasing crown ether concentration and on aging the protein solution. The protein appears to return to its native conformation when it is restored to an aqueous environment.