Peridinin-chlorophyll-protein reconstituted with chlorophyll mixtures: preparation, bulk and single molecule spectroscopy.
FEBS Lett
; 580(22): 5257-62, 2006 Oct 02.
Article
en En
| MEDLINE
| ID: mdl-16962590
Reconstitution of the 16 kDa N-terminal domain of the peridinin-chlorophyll-protein, N-PCP, with mixtures of chlorophyll a (Chl a) and Chl b, resulted in 32 kDa complexes containing two pigment clusters, each bound to one N-PCP. Besides homo-chlorophyllous complexes, hetero-chlorophyllous ones were obtained that contain Chl a in one pigment cluster, and Chl b in the other. Binding of Chl b is stronger than that of the native pigment, Chl a. Energy transfer from Chl b to Chl a is efficient, but there are only weak interactions between the two pigments. Individual homo- and hetero-chlorophyllous complexes were investigated by single molecule spectroscopy using excitation into the peridinin absorption band and scanning of the Chl fluorescence, the latter show frequently well resolved emissions of the two pigments.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Carotenoides
/
Proteínas Protozoarias
/
Clorofila
/
Eucariontes
Límite:
Animals
Idioma:
En
Revista:
FEBS Lett
Año:
2006
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Reino Unido