Molecular basis of photoprotection and control of photosynthetic light-harvesting. Pascal, A. A., Liu, Z., Broess, K., van Oort, B., van Amerongen, H., Wang, C., Horton, P., Robert, B., Chang, W., & Ruban, A. Nature, 436(7047):134–137, July, 2005. doi abstract bibtex In order to maximize their use of light energy in photosynthesis, plants have molecules that act as light-harvesting antennae, which collect light quanta and deliver them to the reaction centres, where energy conversion into a chemical form takes place. The functioning of the antenna responds to the extreme changes in the intensity of sunlight encountered in nature. In shade, light is efficiently harvested in photosynthesis. However, in full sunlight, much of the energy absorbed is not needed and there are vitally important switches to specific antenna states, which safely dissipate the excess energy as heat. This is essential for plant survival, because it provides protection against the potential photo-damage of the photosynthetic membrane. But whereas the features that establish high photosynthetic efficiency have been highlighted, almost nothing is known about the molecular nature of the dissipative states. Recently, the atomic structure of the major plant light-harvesting antenna protein, LHCII, has been determined by X-ray crystallography. Here we demonstrate that this is the structure of a dissipative state of LHCII. We present a spectroscopic analysis of this crystal form, and identify the specific changes in configuration of its pigment population that give LHCII the intrinsic capability to regulate energy flow. This provides a molecular basis for understanding the control of photosynthetic light-harvesting.
@article{pascal_molecular_2005,
title = {Molecular basis of photoprotection and control of photosynthetic light-harvesting},
volume = {436},
issn = {1476-4687},
doi = {10.1038/nature03795},
abstract = {In order to maximize their use of light energy in photosynthesis, plants have molecules that act as light-harvesting antennae, which collect light quanta and deliver them to the reaction centres, where energy conversion into a chemical form takes place. The functioning of the antenna responds to the extreme changes in the intensity of sunlight encountered in nature. In shade, light is efficiently harvested in photosynthesis. However, in full sunlight, much of the energy absorbed is not needed and there are vitally important switches to specific antenna states, which safely dissipate the excess energy as heat. This is essential for plant survival, because it provides protection against the potential photo-damage of the photosynthetic membrane. But whereas the features that establish high photosynthetic efficiency have been highlighted, almost nothing is known about the molecular nature of the dissipative states. Recently, the atomic structure of the major plant light-harvesting antenna protein, LHCII, has been determined by X-ray crystallography. Here we demonstrate that this is the structure of a dissipative state of LHCII. We present a spectroscopic analysis of this crystal form, and identify the specific changes in configuration of its pigment population that give LHCII the intrinsic capability to regulate energy flow. This provides a molecular basis for understanding the control of photosynthetic light-harvesting.},
language = {eng},
number = {7047},
journal = {Nature},
author = {Pascal, Andrew A. and Liu, Zhenfeng and Broess, Koen and van Oort, Bart and van Amerongen, Herbert and Wang, Chao and Horton, Peter and Robert, Bruno and Chang, Wenrui and Ruban, Alexander},
month = jul,
year = {2005},
pmid = {16001075},
keywords = {Chlorophyll, Crystallization, Crystallography, X-Ray, Fluorescence, Light-Harvesting Protein Complexes, Models, Molecular, Photosystem II Protein Complex, Pigments, Biological, Protein Structure, Tertiary, Spectrum Analysis, Raman, Structure-Activity Relationship, light, photosynthesis, plants},
pages = {134--137},
}
Downloads: 0
{"_id":"asTBr6m8DcCQ5N6hJ","bibbaseid":"pascal-liu-broess-vanoort-vanamerongen-wang-horton-robert-etal-molecularbasisofphotoprotectionandcontrolofphotosyntheticlightharvesting-2005","authorIDs":["5cead58d66f5d0da01000080"],"author_short":["Pascal, A. A.","Liu, Z.","Broess, K.","van Oort, B.","van Amerongen, H.","Wang, C.","Horton, P.","Robert, B.","Chang, W.","Ruban, A."],"bibdata":{"bibtype":"article","type":"article","title":"Molecular basis of photoprotection and control of photosynthetic light-harvesting","volume":"436","issn":"1476-4687","doi":"10.1038/nature03795","abstract":"In order to maximize their use of light energy in photosynthesis, plants have molecules that act as light-harvesting antennae, which collect light quanta and deliver them to the reaction centres, where energy conversion into a chemical form takes place. The functioning of the antenna responds to the extreme changes in the intensity of sunlight encountered in nature. In shade, light is efficiently harvested in photosynthesis. However, in full sunlight, much of the energy absorbed is not needed and there are vitally important switches to specific antenna states, which safely dissipate the excess energy as heat. This is essential for plant survival, because it provides protection against the potential photo-damage of the photosynthetic membrane. But whereas the features that establish high photosynthetic efficiency have been highlighted, almost nothing is known about the molecular nature of the dissipative states. Recently, the atomic structure of the major plant light-harvesting antenna protein, LHCII, has been determined by X-ray crystallography. Here we demonstrate that this is the structure of a dissipative state of LHCII. We present a spectroscopic analysis of this crystal form, and identify the specific changes in configuration of its pigment population that give LHCII the intrinsic capability to regulate energy flow. This provides a molecular basis for understanding the control of photosynthetic light-harvesting.","language":"eng","number":"7047","journal":"Nature","author":[{"propositions":[],"lastnames":["Pascal"],"firstnames":["Andrew","A."],"suffixes":[]},{"propositions":[],"lastnames":["Liu"],"firstnames":["Zhenfeng"],"suffixes":[]},{"propositions":[],"lastnames":["Broess"],"firstnames":["Koen"],"suffixes":[]},{"propositions":["van"],"lastnames":["Oort"],"firstnames":["Bart"],"suffixes":[]},{"propositions":["van"],"lastnames":["Amerongen"],"firstnames":["Herbert"],"suffixes":[]},{"propositions":[],"lastnames":["Wang"],"firstnames":["Chao"],"suffixes":[]},{"propositions":[],"lastnames":["Horton"],"firstnames":["Peter"],"suffixes":[]},{"propositions":[],"lastnames":["Robert"],"firstnames":["Bruno"],"suffixes":[]},{"propositions":[],"lastnames":["Chang"],"firstnames":["Wenrui"],"suffixes":[]},{"propositions":[],"lastnames":["Ruban"],"firstnames":["Alexander"],"suffixes":[]}],"month":"July","year":"2005","pmid":"16001075","keywords":"Chlorophyll, Crystallization, Crystallography, X-Ray, Fluorescence, Light-Harvesting Protein Complexes, Models, Molecular, Photosystem II Protein Complex, Pigments, Biological, Protein Structure, Tertiary, Spectrum Analysis, Raman, Structure-Activity Relationship, light, photosynthesis, plants","pages":"134–137","bibtex":"@article{pascal_molecular_2005,\n\ttitle = {Molecular basis of photoprotection and control of photosynthetic light-harvesting},\n\tvolume = {436},\n\tissn = {1476-4687},\n\tdoi = {10.1038/nature03795},\n\tabstract = {In order to maximize their use of light energy in photosynthesis, plants have molecules that act as light-harvesting antennae, which collect light quanta and deliver them to the reaction centres, where energy conversion into a chemical form takes place. The functioning of the antenna responds to the extreme changes in the intensity of sunlight encountered in nature. In shade, light is efficiently harvested in photosynthesis. However, in full sunlight, much of the energy absorbed is not needed and there are vitally important switches to specific antenna states, which safely dissipate the excess energy as heat. This is essential for plant survival, because it provides protection against the potential photo-damage of the photosynthetic membrane. But whereas the features that establish high photosynthetic efficiency have been highlighted, almost nothing is known about the molecular nature of the dissipative states. Recently, the atomic structure of the major plant light-harvesting antenna protein, LHCII, has been determined by X-ray crystallography. Here we demonstrate that this is the structure of a dissipative state of LHCII. We present a spectroscopic analysis of this crystal form, and identify the specific changes in configuration of its pigment population that give LHCII the intrinsic capability to regulate energy flow. This provides a molecular basis for understanding the control of photosynthetic light-harvesting.},\n\tlanguage = {eng},\n\tnumber = {7047},\n\tjournal = {Nature},\n\tauthor = {Pascal, Andrew A. and Liu, Zhenfeng and Broess, Koen and van Oort, Bart and van Amerongen, Herbert and Wang, Chao and Horton, Peter and Robert, Bruno and Chang, Wenrui and Ruban, Alexander},\n\tmonth = jul,\n\tyear = {2005},\n\tpmid = {16001075},\n\tkeywords = {Chlorophyll, Crystallization, Crystallography, X-Ray, Fluorescence, Light-Harvesting Protein Complexes, Models, Molecular, Photosystem II Protein Complex, Pigments, Biological, Protein Structure, Tertiary, Spectrum Analysis, Raman, Structure-Activity Relationship, light, photosynthesis, plants},\n\tpages = {134--137},\n}\n\n","author_short":["Pascal, A. A.","Liu, Z.","Broess, K.","van Oort, B.","van Amerongen, H.","Wang, C.","Horton, P.","Robert, B.","Chang, W.","Ruban, A."],"key":"pascal_molecular_2005","id":"pascal_molecular_2005","bibbaseid":"pascal-liu-broess-vanoort-vanamerongen-wang-horton-robert-etal-molecularbasisofphotoprotectionandcontrolofphotosyntheticlightharvesting-2005","role":"author","urls":{},"keyword":["Chlorophyll","Crystallization","Crystallography","X-Ray","Fluorescence","Light-Harvesting Protein Complexes","Models","Molecular","Photosystem II Protein Complex","Pigments","Biological","Protein Structure","Tertiary","Spectrum Analysis","Raman","Structure-Activity Relationship","light","photosynthesis","plants"],"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/zotero/adrienthurotte","creationDate":"2019-05-26T18:06:05.822Z","downloads":0,"keywords":["chlorophyll","crystallization","crystallography","x-ray","fluorescence","light-harvesting protein complexes","models","molecular","photosystem ii protein complex","pigments","biological","protein structure","tertiary","spectrum analysis","raman","structure-activity relationship","light","photosynthesis","plants"],"search_terms":["molecular","basis","photoprotection","control","photosynthetic","light","harvesting","pascal","liu","broess","van oort","van amerongen","wang","horton","robert","chang","ruban"],"title":"Molecular basis of photoprotection and control of photosynthetic light-harvesting","year":2005,"dataSources":["FLomE5jy47WaXFA6a","MQg4y2ke6Pj8nXrzF"]}