Complete Thermal-Unfolding Profiles of Oxidized and Reduced Cytochromes c

• DOI: 10.1021/ja046667t
• Publication Date: 2004-11-10T05:59:55Z
• Authors: Susumu Uchiyama; Atsushi Ohshima; Shota Nakamura; Jun Hasegawa; Norifumi Terui; Shin-ichi Joseph ...; Yasuhiko Yamamoto; Yoshihiro Sambongi; Yuji Kobayashi
• Keywords: 0301 basic medicine; Protein Folding; 0303 health sciences; 03 medical and health sciences; Hot Temperature; Circular Dichroism; Cytochromes c; Thermodynamics; Oxidation-Reduction

The complete thermal-unfolding profiles of both oxidized and reduced forms of cytochrome c551 (PA) from mesophilic Pseudomonas aeruginosa and cytochrome c552 (HT) from thermophilic Hydrogenobacter thermophilus were obtained by the newly developed pressure-proof cell compartment installed in a circular dichroic spectrometer, which facilitates protein thermal-unfolding experiments up to 180 degrees C. The thermodynamic cycle, which relates protein stability and redox function, indicated that the redox potentials of PA and HT in the native state are regulated by the stability of the oxidized proteins rather than by that of the reduced ones.