Multiple types of association of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes

EJ Boekema, H van Roon, F Calkoen, R Bassi, JP Dekker*, Jan P. Dekker

*Corresponding author for this work

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169 Citations (Scopus)
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Abstract

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-alpha,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) FEES 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.

Original languageEnglish
Pages (from-to)2233-2239
Number of pages7
JournalBiochemistry
Volume38
Issue number8
DOIs
Publication statusPublished - 23-Feb-1999

Keywords

  • SPINACH THYLAKOID MEMBRANES
  • A/B-BINDING-PROTEINS
  • GREEN PLANTS
  • BIOCHEMICAL-CHARACTERIZATION
  • ELECTRON CRYSTALLOGRAPHY
  • 3-DIMENSIONAL STRUCTURE
  • IN-VIVO
  • COMPLEX
  • ORGANIZATION
  • RESOLUTION

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