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:15535669
Additional Information

Study Summary

Number of data points 16
Proteins Cytochrome c-552 ; Cytochrome c-551 ; Cytochrome c-552 ; Cytochrome c-551
Unique complexes 2
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 NEQLAKQKGCMACHDLKAKKVGPAYADVAKKYAGRKDAVDYLAGKIKKGGSGVWGSVPMPPQNVTDAEAKQLAQWILSIK ; Mutations for sequence EDPEVLFKNKGCVACHAIDTKMVGPAYKDVAAKFAGQAGAEAELAQRIKNGSQGVWGPIPMPPNAVSDDEAQTLAKWVLSQK

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 PDB Entries

Structure ID Release Date Resolution Structure Title
2PAC 1993-10-31 SOLUTION STRUCTURE OF FE(II) CYTOCHROME C551 FROM PSEUDOMONAS AERUGINOSA AS DETERMINED BY TWO-DIMENSIONAL 1H NMR
2AI5 2006-05-23 Solution Structure of Cytochrome C552, determined by Distributed Computing Implementation for NMR data
1AYG 1998-11-25 SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES
1DVV 2000-11-29 SOLUTION STRUCTURE OF THE QUINTUPLE MUTANT OF CYTOCHROME C-551 FROM PSEUDOMONAS AERUGINOSA
5XEC 2017-08-09 1.1 Heterodimer constructed from PA cyt c551-HT cyt c552 and HT cyt c552-PA cyt c551 chimeric proteins
5AUR 2015-10-21 1.26 Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at N-terminal region
5AUS 2015-10-21 1.3 Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at C-terminal region
3X39 2015-04-22 1.5 Domain-swapped dimer of Pseudomonas aeruginosa cytochrome c551
5XED 2017-08-09 1.55 Heterodimer constructed from M61A PA cyt c551-HT cyt c552 and HT cyt c552-PA cyt c551 chimeric proteins
451C 1981-10-02 1.6 STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS
351C 1981-10-02 1.6 STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS
4ZID 2016-02-10 1.8 Dimeric Hydrogenobacter thermophilus cytochrome c552 obtained from Escherichia coli
2EXV 2006-02-07 1.86 Crystal structure of the F7A mutant of the cytochrome c551 from Pseudomonas aeruginosa
1YNR 2005-05-17 2.0 Crystal structure of the cytochrome c-552 from Hydrogenobacter thermophilus at 2.0 resolution
3VYM 2012-11-07 2.0 Dimeric Hydrogenobacter thermophilus cytochrome c552

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