Multiple Types of Association of Photosystem II and Its Light-Harvesting Antenna in Partially Solubilized Photosystem II Membranes

• Published in: Biochemistry (Easton) 1999-02, Vol.38 (8), p.2233-2239
• Main Authors: Boekema, Egbert J, van Roon, Henny, Calkoen, Florentine, Bassi, Roberto, Dekker, Jan P
• Format: Article
• Language: English
• Subjects: Chloroplasts - chemistry; Chloroplasts - ultrastructure; FOTOSINTESIS; Image Processing, Computer-Assisted; Intracellular Membranes - chemistry; Intracellular Membranes - ultrastructure; LIGHT; LIGHT HARVESTING COMPLEXES; Light-Harvesting Protein Complexes; LUMIERE; LUZ; Macromolecular Substances; PHOTOSYNTHESE; PHOTOSYNTHESIS; Photosynthetic Reaction Center Complex Proteins - chemistry; Photosynthetic Reaction Center Complex Proteins - ultrastructure; Photosystem II Protein Complex; PROTEINAS; PROTEINE; PROTEINS; Software; Solubility; Spinacia oleracea
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi9827161

Photosystem II is a multisubunit pigment−protein complex embedded in the thylakoid membranes of chloroplasts. It utilizes light for photochemical energy conversion, and is heavily involved in the regulation of the energy flow. We investigated the structural organization of photosystem II and its associated light-harvesting antenna by electron microscopy, multivariate statistical analysis, and classification procedures on partially solubilized photosystem II membranes from spinach. Observation by electron microscopy shortly after a mild disruption of freshly prepared membranes with the detergent n-dodecyl-α,d-maltoside revealed the presence of several large supramolecular complexes. In addition to the previously reported supercomplexes [Boekema, E. J., van Roon, H., and Dekker, J. P. (1998) FEBS Lett. 424, 95−99], we observed complexes with the major trimeric chlorophyll a/b protein (LHCII) in a third, L-type of binding position (C2S2M0 - 2L1 - 2), and two different types of megacomplexes, both identified as dimeric associations of supercomplexes with LHCII in two types of binding sites (C4S4M2 - 4). We conclude that the association of photosystem II and its associated light-harvesting antenna is intrinsically heterogeneous, and that the minor CP26 and CP24 proteins play a crucial role in the supramolecular organization of the complete photosystem. We suggest that different types of organization form the structural basis for photosystem II to specifically react to changing light and stress conditions, by providing different routes of excitation energy transfer.