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. Study holds ProTherm entries: 20146, 20147, 20148, 20149, 20150, 20151, 20152, 20153 Extra Details: Oxidized form. cytochrome c, oxidiced, reduced, thermal unfolding,
Submission Details
ID: 3MHUSzFx
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:15535669Additional Information
Study Summary
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Data Distribution
Studies with similar sequences (approximate matches)