Complete thermal-unfolding profiles of oxidized and reduced cytochromes C.


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. Study holds ProTherm entries: 20146, 20147, 20148, 20149, 20150, 20151, 20152, 20153 Extra Details: Oxidized form. cytochrome c, oxidiced, reduced, thermal unfolding,

Submission Details


Submitter: Connie Wang

Submission Date: April 24, 2018, 8:52 p.m.

Version: 1

Publication Details
Uchiyama S;Ohshima A;Nakamura S;Hasegawa J;Terui N;Takayama SJ;Yamamoto Y;Sambongi Y;Kobayashi Y,J. Am. Chem. Soc. (2004) Complete thermal-unfolding profiles of oxidized and reduced cytochromes C. PMID:15535669
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Cytochrome c-552 P15452 CY552_HYDTT
100.0 Cytochrome c-551 P00099 CY551_PSEAE