Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c

被引：56

作者：

Ferri, T

Poscia, A

Ascoli, F

Santucci, R

机构：

[1] UNIV ROMA TOR VERGATA,DIPARTIMENTO MED SPERIMENTALE & SCI BIOCHIM,I-00133 ROME,ITALY

[2] UNIV ROMA LA SAPIENZA,DIPARTIMENTO CHIM,I-00185 ROME,ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1996年 / 1298卷 / 01期

关键词：

cytochrome c; hemoprotein; unfolding intermediate; voltammetry; circular dichroism;

D O I：

10.1016/S0167-4838(96)00122-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：102 / 108

页数：7

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