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
em 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.
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Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Monóxido de Carbono
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Espectroscopia de Infravermelho com Transformada de Fourier
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Complexo IV da Cadeia de Transporte de Elétrons
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Proteínas de Saccharomyces cerevisiae
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Mutação
Limite:
Animals
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article