T. Ferri et al., DIRECT ELECTROCHEMICAL EVIDENCE FOR AN EQUILIBRIUM INTERMEDIATE IN THE GUANIDINE-INDUCED UNFOLDING OF CYTOCHROME-C, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1298(1), 1996, pp. 102-108
This paper reports a voltammetric and spectroscopic investigation of t
he guanidine-induced unfolding of cytochrome c at neutral pH and 25 de
grees C. Electrochemical data provide direct evidence for the presence
of an equilibrium intermediate (form I) strictly dependent on the den
aturant concentration. The midpoint potential of farm I has been deter
mined (E(1/2) = +0.010 V vs. NHE) and its structural features defined
rom analysis of the circular dichroism and absorbance spectroscopy dat
a obtained under the same experimental conditions. From the correlatio
n of electrochemical and spectroscopic data, we propose that the featu
res detected by the intermediate conform to the molten globule state.