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,
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:52 p.m.
|Number of data points||16|
|Proteins||Cytochrome c-552 ; Cytochrome c-551 ; Cytochrome c-552 ; Cytochrome c-551|
|Assays/Quantities/Protocols||Experimental Assay: dG units:kcal/mol ; Experimental Assay: dHvH temp:25.0 C ; Experimental Assay: dG units:kJ/mol ; Experimental Assay: Tm ; Experimental Assay: dHvH|
|Libraries||Mutations for sequence EDPEVLFKNKGCVACHAIDTKMVGPAYKDVAAKFAGQAGAEAELAQRIKNGSQGVWGPIPMPPNAVSDDEAQTLAKWVLSQK ; Mutations for sequence NEQLAKQKGCMACHDLKAKKVGPAYADVAKKYAGRKDAVDYLAGKIKKGGSGVWGSVPMPPQNVTDAEAKQLAQWILSIK|