Uchiyama Susumu, Ohshima Atsushi, Nakamura Shota, Hasegawa Jun, Terui Norifumi, Takayama Shin-ichi Joseph, Yamamoto Yasuhiko, Sambongi Yoshihiro, Kobayashi Yuji
Graduate School of Pharmaceutical Sciences, Osaka University, Suita 565-0871, Japan.
J Am Chem Soc. 2004 Nov 17;126(45):14684-5. doi: 10.1021/ja046667t.
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.
