Characterization of the pH-dependent resonance Raman transitions of archaeal and bacterial Rieske [2Fe-2S] proteins.
J Am Chem Soc
; 126(15): 4788-9, 2004 Apr 21.
Article
en En
| MEDLINE
| ID: mdl-15080677
ABSTRACT
The pH-dependent resonance Raman (RR) spectral changes of the cytochrome bc1-associated, high-potential Rieske proteins have frequently been invoked to explain the redox-linked ionization behavior. We report herein RR spectral data of archaeal and bacterial Rieske proteins that directly demonstrate the pH-dependent changes near and above pKa,ox2, but not around pKa,ox1, of the visible circular dichroism (CD) transitions. The RR spectral changes are attributed to modification of the immediate [2Fe-2S] cluster environment due to deprotonation of some exchangeable amide groups in the polypeptide backbone, rather than previously assumed simple changes of the Fe-Nimid stretching vibrations.
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Bases de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Complejo III de Transporte de Electrones
/
Proteínas Arqueales
/
Proteínas Hierro-Azufre
Idioma:
En
Revista:
J Am Chem Soc
Año:
2004
Tipo del documento:
Article
País de afiliación:
Japón