Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c.
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 form I has been determined (E1/2 = +0.010 V vs. NHE) and its structural features defined from 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
T
Dipartimento di Chimica, Università di Roma La Sapienza, Italy.
Poscia
A
A
Ascoli
F
F
Santucci
R
R
D000818:Animals; D002942:Circular Dichroism; D003574:Cytochrome c Group / Q000737:chemistry* / Q000187:drug effects; D004563:Electrochemistry; D004579:Electron Transport; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology*; D006420:Hemeproteins / Q000187:drug effects / Q000378:metabolism; D006736:Horses; D009206:Myocardium / Q000737:chemistry; D010084:Oxidation-Reduction; D011489:Protein Denaturation; D017510:Protein Folding; D013053:Spectrophotometry
D003574:Cytochrome c Group; D006146:Guanidines; D006420:Hemeproteins; D019791:Guanidine