Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/121151
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Detergent-induced reversible denaturation of the photosystem II reaction center: Implications for pigment-protein interactions |
Autor: | Montoya Blanco, Guillermo; Cases, Rafael CSIC; Rodríguez, Rosalía; Aured Galve, María CSIC; Picorel Castaño, Rafael CSIC ORCID | Fecha de publicación: | 1994 | Editor: | American Chemical Society | Citación: | Biochemistry 33: 11798-11804 (1994) | Resumen: | Incubation of the D1-D2-cytochrome b559 complex with Triton X-100 modified the protein secondary structure, caused significant spectral modifications, and reduced the formation of light-induced spin-polarized triplet electron paramagnetic resonance (EPR) signal. After 24 h of incubation, the absorption spectrum shifted from 675.5 to 671.5 nm and the fluorescence spectrum shifted from 682 to 672 nm. These shifts were accompanied by an increase in the chlorophyll fluorescence yield and by decreases in the intensity of the circular dichroism in the red region and the secondary electron transport activity. The intensity of the light-induced triplet EPR signal was also markedly reduced in the same experimental conditions. Substitution of dodecyl β-maltoside for Triton X-100 reversed all the above-mentioned parameters to the values exhibited by the native D1-D2-Cyt b559 complex, including the characteristic triplet EPR signal. We concluded that all observed changes were due to the destruction of P680 with Triton X-100 and to the reestablishment of P680 in the presence of dodecyl β-maltoside. The easier but certainly not the only possible explanation to all these phenomena is to consider a dimeric structure for P680, at least in its ground state, where interactions take place within the two dimeric chromophores and with the apoprotein. Such a dimeric structure would be very sensitive to small modifications of the P680 domain, which convert the dimer absorbing at 680 into two chlorophyll monomers absorbing near 670 nm. The dodecyl β-maltoside reestablished the structure of the native P680 domain. | URI: | http://hdl.handle.net/10261/121151 | DOI: | 10.1021/bi00205a016 | Identificadores: | doi: 10.1021/bi00205a016 issn: 0006-2960 |
Aparece en las colecciones: | (EEAD) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
17
checked on 20-abr-2024
WEB OF SCIENCETM
Citations
16
checked on 27-feb-2024
Page view(s)
340
checked on 24-abr-2024
Download(s)
106
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.