Distribution of the chlorophyll spectral forms in the chlorophyll-protein complexes of photosystem II antenna

The precise nature of interactions between the chloropnyll-protein complexes related to photosystem I or photosystem II and the acyl lipids in the thylakoid membranes is not yet fully elucidated. Analyses of the lipid content of isolated photosystem supramolecular complexes reveal that they are integral components of these complexes. However, the relations between certain acyl lipids and the specific structure and functions of the complexes investigated are still widely discussed. The most generally accepted phenomenon is the fact of participation of phosphatidylglycerol containing the unique <em>trans-</em>Δ<sup>3</sup> -hexadecenoic acid in the oligomerization of the light-harvesting chlorophyll a/b protein complex II.

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Orientation of the pigments in Photosystem II: A low-temperature linear dichroism and polarized fluorescence emission study of chlorophyll-protein complexes isolated from Chlamydomonas reinhardtii

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/0005-2728(86)90020-4 ◽

1986 ◽

Vol 850 (1) ◽

pp. 156-161 ◽

Cited By ~ 25

Author(s):

P. Tapie ◽

Y. Choquet ◽

F.-A. Wollman ◽

B. Diner ◽

J. Breton

Keyword(s):

Low Temperature ◽

Photosystem Ii ◽

Chlamydomonas Reinhardtii ◽

Protein Complexes ◽

Fluorescence Emission ◽

Linear Dichroism ◽

Polarized Fluorescence ◽

Chlorophyll Protein Complexes ◽

Chlorophyll Protein ◽

Emission Study

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Structural changes and lateral redistribution of photosystem II during donor side photoinhibition of thylakoids.

The Journal of Cell Biology ◽

10.1083/jcb.119.2.325 ◽

1992 ◽

Vol 119 (2) ◽

pp. 325-335 ◽

Cited By ~ 114

Author(s):

R Barbato ◽

G Friso ◽

F Rigoni ◽

F Dalla Vecchia ◽

G M Giacometti

Keyword(s):

Photosystem Ii ◽

Photosystem I ◽

Structural Changes ◽

Protein Complexes ◽

Gradient Centrifugation ◽

Photosynthetic Apparatus ◽

Topological Stability ◽

Donor Side ◽

Chlorophyll Protein Complexes ◽

Chlorophyll Protein

The structural and topological stability of thylakoid components under photoinhibitory conditions (4,500 microE.m-2.s-1 white light) was studied on Mn depleted thylakoids isolated from spinach leaves. After various exposures to photoinhibitory light, the chlorophyll-protein complexes of both photosystems I and II were separated by sucrose gradient centrifugation and analysed by Western blotting, using a set of polyclonals raised against various apoproteins of the photosynthetic apparatus. A series of events occurring during donor side photoinhibition are described for photosystem II, including: (a) lowering of the oligomerization state of the photosystem II core; (b) cleavage of 32-kD protein D1 at specific sites; (c) dissociation of chlorophyll-protein CP43 from the photosystem II core; and (d) migration of damaged photosystem II components from the grana to the stroma lamellae. A tentative scheme for the succession of these events is illustrated. Some effects of photoinhibition on photosystem I are also reported involving dissociation of antenna chlorophyll-proteins LHCI from the photosystem I reaction center.

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