Supramolecular structure of the photosystem II complex from green plants and cyanobacteria

Boekema, EJ, Hankamer, B, Bald, D, Kruip, J, Nield, J, Boonstra, AF, Barber, J and Rogner, M (1995) Supramolecular structure of the photosystem II complex from green plants and cyanobacteria. Proceedings of the National Academy of Sciences of the United States of America, 92 1: 175-179. doi:10.1073/pnas.92.1.175


Author Boekema, EJ
Hankamer, B
Bald, D
Kruip, J
Nield, J
Boonstra, AF
Barber, J
Rogner, M
Title Supramolecular structure of the photosystem II complex from green plants and cyanobacteria
Journal name Proceedings of the National Academy of Sciences of the United States of America   Check publisher's open access policy
ISSN 0027-8424
Publication date 1995-01-03
Year available 1995
Sub-type Article (original research)
DOI 10.1073/pnas.92.1.175
Open Access Status Not yet assessed
Volume 92
Issue 1
Start page 175
End page 179
Total pages 5
Place of publication WASHINGTON
Publisher NATL ACAD SCIENCES
Language eng
Subject 1311 Genetics
1000 General
Abstract Photosystem II (PSII) complexes, isolated from spinach and the thermophilic cyanobacterium Synechococcus elongatus, were characterized by electron microscopy and single-particle image-averaging analyses. Oxygen-evolving core complexes from spinach and Synechococcus having molecular masses of about 450 kDa and dimensions of approximate to 17.2 x 9.7 nm showed twofold symmetry indicative of a dimeric organization. Confirmation of this came from image analysis of oxygen evolving monomeric cores of PSII isolated from spinach and Synechococcus having a mass of approximate to 240 kDa. Washing with Tris at pH 8.0 and analysis of side-view projections indicated the possible position of the 33-kDa extrinsic manganese-stabilizing protein. A larger complex was isolated that contained the light-harvesting complex II (LHC-II) and other chlorophyll a/b-binding proteins, CP29, CP26, and CP24. This LHC-II-PSII complex had a mass of about 700 kDa, and electron microscopy revealed it also to be a dimer having dimensions of about 26.8 and 12.3 nm. From comparison with the dimeric core complex, it was deduced that the latter is located in the center of the larger particle, with additional peripheral regions accommodating the chlorophyll a/b-binding proteins. It is suggested that two LHC-II trimers are present in each dimeric LHC-II-PSII complex and that each trimer is linked to the reaction center core complex by CP24, CP26, and CP29. The results also suggest that PSII may exist as a dimer in vivo.
Keyword image analysis
subunit positioning
transmission electron microscopy
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
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