Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.
Biochim Biophys Acta Bioenerg
; 1859(9): 705-711, 2018 09.
Article
in En
| MEDLINE
| ID: mdl-29852141
ABSTRACT
Redox and CO photolysis FTIR spectra of yeast cytochrome c oxidase WT and mutants are compared to those from bovine and P. denitrificans CcOs in order to establish common functional features. All display changes that can be assigned to their E242 (bovine numbering) equivalent and to weakly H-bonded water molecules. The additional redox-sensitive band reported at 1736â¯cm-1 in bovine CcO and previously assigned to D51 is absent from yeast CcO and couldn't be restored by introduction of a D residue at the equivalent position of the yeast protein. Redox spectra of yeast CcO also show much smaller changes in the amide I region, which may relate to structural differences in the region around D51 and the subunit I/II interface.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Saccharomyces cerevisiae
/
Carbon Monoxide
/
Spectroscopy, Fourier Transform Infrared
/
Electron Transport Complex IV
/
Saccharomyces cerevisiae Proteins
/
Mutation
Limits:
Animals
Language:
En
Journal:
Biochim Biophys Acta Bioenerg
Year:
2018
Type:
Article