Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes
Autor: | Boekema, EJ, van Roon, H, van Breemen, JFL, Dekker, JP, Dekker, Jan P. |
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Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology, Electron Microscopy, Biophysics Photosynthesis/Energy |
Jazyk: | angličtina |
Rok vydání: | 1999 |
Předmět: |
Photosystem II
GREEN PLANTS PROTEINS Photosynthetic Reaction Center Complex Proteins Light-Harvesting Protein Complexes Trimer Photosystem I Biochemistry Models Biological Thylakoids Light-harvesting complex Bacterial Proteins Spinacia oleracea BINDING PARTICLES SDG 7 - Affordable and Clean Energy Binding site 3-DIMENSIONAL STRUCTURE IN-VIVO Plant Proteins SPINACH light harvesting complex P700 COMPLEX PURIFICATION electron microscopy Chemistry Photosystem II Protein Complex photosystem II thylakoid membrane Crystallography Microscopy Electron Membrane RESOLUTION Thylakoid Chlorophyll Binding Proteins Dimerization |
Zdroj: | European Journal of Biochemistry, 266(2), 444-452. Blackwell Publishing Ltd European Journal of Biochemistry, 266, 444-452. Wiley-Blackwell Boekema, E J, van Roon, H, van Breemen, J F L & Dekker, J P 1999, ' Supramolecular organization of photosystem II and its associated light-harvesting antenna in partially solubilized hotosystem II membranes ', European Journal of Biochemistry, vol. 266, pp. 444-452 . https://doi.org/10.1046/j.1432-1327.1999.00876.x |
ISSN: | 0014-2956 |
Popis: | We present an extended analysis of the organization of green plant photosystem II and its associated light-harvesting antenna using electron microscopy and image analysis. The analysis is based on a large dataset of 16 600 projections of negatively stained PSII-LHCII supercomplexes and megacomplexes prepared by means of three different pretreatments. In addition to our previous work on this system [Boekema, E.J., van Roon, H., Calkoen, F., Bassi, R. and Dekker, J.P. (1999) Biochemistry 38, 2233-2239], the following results were obtained.The rotational orientation of trimeric LHCII at the S, M and L binding positions was determined. It was found that compared to the S trimer, the M and L trimers are rotationally shifted by about -20 degrees and -50 degrees, respectively.The number of projections with empty CP29, CP26 and CP24 binding sites was found to be about 0, 18 and 4%, respectively. We suggest that CP26 and CP24 are not required for the binding of trimeric LHCII at any of the three binding positions.A new type of megacomplex was observed with a characteristic windmill-like shape. This type III megacomplex consists of two C2S2 supercomplexes connected at their CP26 tips.Structural variation in the region of the central dimeric photosystem II complex was found to occur at one specific position near the periphery of the complex. We attribute this variation to the partial absence of an extrinsic polypeptide or one or more small intrinsic membrane proteins. |
Databáze: | OpenAIRE |
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