This paper reports a voltammetric and spectroscopic investigation of the guanidine-induced unfolding of cytochrome c at neutral pH and 25 degrees C. Electrochemical data provide direct evidence for the presence of an equilibrium intermediate (form I) strictly dependent on the denaturant concentration. The midpoint potential of farm I has been determined (E(1/2) = +0.010 V vs. NHE) and its structural features defined rom analysis of the circular dichroism and absorbance spectroscopy data obtained under the same experimental conditions. From the correlation of electrochemical and spectroscopic data, we propose that the features detected by the intermediate conform to the molten globule state.
Ferri, T., Poscia, A., Ascoli, F., Santucci, R. (1996). 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), 102-108 [10.1016/S0167-4838(96)00122-7].
Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c
SANTUCCI, ROBERTO
1996-01-01
Abstract
This paper reports a voltammetric and spectroscopic investigation of the guanidine-induced unfolding of cytochrome c at neutral pH and 25 degrees C. Electrochemical data provide direct evidence for the presence of an equilibrium intermediate (form I) strictly dependent on the denaturant concentration. The midpoint potential of farm I has been determined (E(1/2) = +0.010 V vs. NHE) and its structural features defined rom analysis of the circular dichroism and absorbance spectroscopy data obtained under the same experimental conditions. From the correlation of electrochemical and spectroscopic data, we propose that the features detected by the intermediate conform to the molten globule state.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
