Article
- The EMBO Journal (2005) 24, 919 - 928
- doi:10.1038/sj.emboj.7600585
Published online: 17 February 2005
Subject Categories:
Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution
Jörg Standfuss1,a, Anke C Terwisscha van Scheltinga1,a, Matteo Lamborghini1 and Werner Kühlbrandt1
- Max Planck Institute of Biophysics, Department of Structural Biology, Frankfurt am Main, Germany
Correspondence to:
Werner Kühlbrandt, Max Planck Institute of Biophysics, Department of Structural Biology, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany. Tel.: +49 69 6303 3001; Fax: +49 69 6303 3002; E-mail: werner.kuehlbrandt@mpibp-frankfurt.mpg.de
aThese authors contributed equally to this work
Received 25 October 2004; Accepted 26 January 2005
Abstract
The plant light-harvesting complex of photosystem II (LHC-II) collects and transmits solar energy for photosynthesis in chloroplast membranes and has essential roles in regulation of photosynthesis and in photoprotection. The 2.5 Å structure of pea LHC-II determined by X-ray crystallography of stacked two-dimensional crystals shows how membranes interact to form chloroplast grana, and reveals the mutual arrangement of 42 chlorophylls a and b, 12 carotenoids and six lipids in the LHC-II trimer. Spectral assignment of individual chlorophylls indicates the flow of energy in the complex and the mechanism of photoprotection in two close chlorophyll a–lutein pairs. We propose a simple mechanism for the xanthophyll-related, slow component of nonphotochemical quenching in LHC-II, by which excess energy is transferred to a zeaxanthin replacing violaxanthin in its binding site, and dissipated as heat. Our structure shows the complex in a quenched state, which may be relevant for the rapid, pH-induced component of nonphotochemical quenching.
Keywords:
- crystal structure,
- energy transfer,
- light harvesting,
- membrane protein,
- photosynthesis
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