Structural characterization of a complex of photosystem I and light-harvesting complex II of Arabidopsis thaliana.
Biochemistry
; 44(33): 10935-40, 2005 Aug 23.
Article
em En
| MEDLINE
| ID: mdl-16101276
ABSTRACT
Chloroplasts are central to the provision of energy for green plants. Their photosynthetic membrane consists of two major complexes converting sunlight photosystem I (PSI) and photosystem II (PSII). The energy flow toward both photosystems is regulated by light-harvesting complex II (LHCII), which after phosphorylation can move from PSII to PSI in the so-called state 1 to state 2 transition and can move back to PSII after dephosphorylation. To investigate the changes of PSI and PSII during state transitions, we studied the structures and frequencies of all major membrane complexes from Arabidopsis thaliana chloroplasts at conditions favoring either state 1 or state 2. We solubilized thylakoid membranes with digitonin and analyzed the complete set of complexes immediately after solubilization by electron microscopy and image analysis. Classification indicated the presence of a PSI-LHCII supercomplex consisting of one PSI-LHCI complex and one LHCII trimer, which was more abundant in state 2 conditions. The presence of LHCII was confirmed by excitation spectra of the PSI emission of membranes in state 1 or state 2. The PSI-LHCII complex could be averaged with a resolution of 16 A, showing that LHCII has a specific binding site at the PSI-A, -H, -L, and -K subunits.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Arabidopsis
/
Folhas de Planta
/
Tilacoides
/
Proteínas de Arabidopsis
/
Complexos de Proteínas Captadores de Luz
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Complexo de Proteína do Fotossistema I
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Holanda