title: Complete thermal-unfolding profiles of oxidized and reduced cytochromes C.
abstract: 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.
authors.affiliation: Graduate School of Pharmaceutical Sciences, Osaka University, Suita 565-0871, Japan.
authors.forename: Susumu
authors.initials: S
authors.lastname: Uchiyama
authors.forename: Atsushi
authors.initials: A
authors.lastname: Ohshima
authors.forename: Shota
authors.initials: S
authors.lastname: Nakamura
authors.forename: Jun
authors.initials: J
authors.lastname: Hasegawa
authors.forename: Norifumi
authors.initials: N
authors.lastname: Terui
authors.forename: Shin-ichi Joseph
authors.initials: SJ
authors.lastname: Takayama
authors.forename: Yasuhiko
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Sambongi
authors.forename: Yuji
authors.initials: Y
authors.lastname: Kobayashi
mesh_terms: D002942:Circular Dichroism; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D010084:Oxidation-Reduction; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D045304:Cytochromes c