Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1787, Issue 6, Pages 753-772Publisher
ELSEVIER
DOI: 10.1016/j.bbabio.2009.03.012
Keywords
Photosynthesis; Light-harvesting; Non-photochemical quenching; Electron microscopy; Crystallisation; Membrane protein
Categories
Funding
- Fundacao para a Ciencia e a Tecnologia [SFRH/BD/21440/2005]
- [SFB 472]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/21440/2005] Funding Source: FCT
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The chlorophyll a/b light-harvesting complex of photosystem II (LHC-II) collects most of the solar energy in the biosphere. LHC-II is the prototype of a highly conserved family of membrane proteins that fuels plant photosynthesis in the conversion of excitation energy into biologically useful chemical energy. In addition, LHC-II plays an important role in the organisation of the thylakoid membrane, the structure of the photosynthetic apparatus, the regulation of energy flow between the two photosystems, and in the controlled dissipation of excess excitation energy under light stress. Our current understanding of the sophisticated mechanisms behind each of these processes has profited greatly from the progress made over the past two decades in determining the structure of the complex. This review presents the developments and breakthroughs that ultimately lead to the high-resolution structure of LHC-II. Based on an alignment of the remarkably well engineered and highly conserved LHC polypeptide, we propose several key features of the LHC-II structure that are likely to be present in all members of the LHC family. Finally, some recently proposed mechanisms of energy-dependent non-photochemical quenching (NPQ) are examined from a structural perspective. (C) 2009 Elsevier B.V. All rights reserved.
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