Protein phosphorylation-induced State I-State II transitions are dependent on thylakoid membrane microviscosity.
Arch Biochem Biophys
; 226(1): 145-54, 1983 Oct 01.
Article
en En
| MEDLINE
| ID: mdl-6639047
ABSTRACT
Incorporation of cholesterol hemisuccinate into thylakoid membranes decreased the membrane fluidity as measured by polarized fluorescence from 1,6-diphenyl-1,3,5-hexatriene. Increasing membrane viscosity in this manner did not inhibit the thylakoid membrane protein kinase. In contrast the effects of the protein phosphorylation on State I-State II transitions, which were observed in untreated membranes, were abolished. This observation is interpreted as indicating that protein phosphorylation-induced energy transfer changes are sensitive to membrane viscosity because they might require a lateral migration of the light-harvesting complex serving Photosystem II from grana to stromal lamellae. Cation effects on room- and low-temperature fluorescence emission properties and membrane adhesion were not abolished in these cholesterol hemisuccinate-treated membranes.
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Banco de datos:
MEDLINE
Asunto principal:
Fotosíntesis
/
Proteínas de Plantas
/
Plantas
/
Proteínas Quinasas
/
Cloroplastos
/
Fluidez de la Membrana
/
Proteínas de la Membrana
Idioma:
En
Año:
1983
Tipo del documento:
Article