Supramolecular organization of photosystem I and light‐harvesting complex I in Chlamydomonas reinhardtii

FEBS Letters

Boekema, Egbert J²  van Gorkom, Hans J¹  Yakushevska, Alevtyna E²  Dekker, Jan P³  Keegstra, Wilko²  Germano, Marta³ 

[1] Biophysics Department, Huygens Laboratory, Leiden University, P.O. Box 9504, 2300 RA Leiden, The Netherlands;Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands;Faculty of Sciences, Department of Physics and Astronomy, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands

关键词: Photosystem I;    Light-harvesting complex I;    Electron microscopy;    State transitions;    Chlamydomonas reinhardtii;    β-DM;    n-dodecyl-β-D-maltoside;    Chl;    chlorophyll;    EM;    electron microscopy;    LHCI;    light-harvesting complex I;    MSA;    multivariate statistical analysis;    PSI;    photosystem I;    PSII;    photosystem II;   

DOI  :  10.1016/S0014-5793(02)03100-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We report a structural characterization by electron microscopy and image analysis of a supramolecular complex consisting of photosystem I and light-harvesting complex I from the unicellular green alga Chlamydomonas reinhardtii. The complex is a monomer, has longest dimensions of 21.3 and 18.2 nm in projection, and is significantly larger than the corresponding complex in spinach. Comparison with photosystem I complexes from other organisms suggests that the complex contains about 14 light-harvesting proteins, two or three of which bind at the side of the PSI-H subunit. We suggest that special light-harvesting I proteins play a role in the binding of phosphorylated light-harvesting complex II in state 2.

【 授权许可】

Unknown