| Optimization of light harvesting and photoprotection: molecular mechanisms and physiological consequences. | |
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MedLine Citation:
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PMID: 23148272 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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The distinctive lateral organization of the protein complexes in the thylakoid membrane investigated by Jan Anderson and co-workers is dependent on the balance of various attractive and repulsive forces. Modulation of these forces allows critical physiological regulation of photosynthesis that provides efficient light-harvesting in limiting light but dissipation of excess potentially damaging radiation in saturating light. The light-harvesting complexes (LHCII) are central to this regulation, which is achieved by phosphorylation of stromal residues, protonation on the lumen surface and de-epoxidation of bound violaxanthin. The functional flexibility of LHCII derives from a remarkable pigment composition and configuration that not only allow efficient absorption of light and efficient energy transfer either to photosystem II or photosystem I core complexes, but through subtle configurational changes can also exhibit highly efficient dissipative reactions involving chlorophyll-xanthophyll and/or chlorophyll-chlorophyll interactions. These changes in function are determined at a macroscopic level by alterations in protein-protein interactions in the thylakoid membrane. The capacity and dynamics of this regulation are tuned to different physiological scenarios by the exact protein and pigment content of the light-harvesting system. Here, the molecular mechanisms involved will be reviewed, and the optimization of the light-harvesting system in different environmental conditions described. |
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Authors:
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Peter Horton |
Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Philosophical transactions of the Royal Society of London. Series B, Biological sciences Volume: 367 ISSN: 1471-2970 ISO Abbreviation: Philos. Trans. R. Soc. Lond., B, Biol. Sci. Publication Date: 2012 Dec |
Date Detail:
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Created Date: 2012-11-13 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7503623 Medline TA: Philos Trans R Soc Lond B Biol Sci Country: England |
Other Details:
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Languages: eng Pagination: 3455-65 Citation Subset: IM |
Affiliation:
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Department of Molecular Biology and Biotechnology, University of Sheffield, , Firth Court, Western Bank, Sheffield S10 2TN, UK. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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