Isolation and characterization of vibrational spectra of individual heme active sites in cytochrome bc1 complexes from Rhodobacter capsulatus.
Biochemistry
; 35(39): 12812-9, 1996 Oct 01.
Article
en En
| MEDLINE
| ID: mdl-8841124
Resonance Raman spectra of bc1 complexes and isolated c1 subunit from Rhodobacter capsulatus have been obtained using a variety of excitation wavelengths. Spectra obtained via Q-band excitation of bc1 complexes in different redox states were separated to yield the individual vibrational spectra of each of the three heme active sites. Hemes bH and c1 exhibit vibrational spectra typical of b- and c-type hemes, respectively. In contrast, the spectrum of heme bL is anomalous with respect to those of other hemes b. The isolated spectra were also used to assess the effects of inhibitor binding on the local structural environments of the hemes. Neither antimycin nor myxothiazol binding produces dramatic structural perturbations at the hemes. Heme c1 is completely unaffected by the presence of either inhibitor. The vibrational spectra of hemes bH and bL are slightly altered by antimycin and myxothiazol binding, respectively.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Rhodobacter capsulatus
/
Complejo III de Transporte de Electrones
/
Hemo
Idioma:
En
Revista:
Biochemistry
Año:
1996
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos