A pigment-binding protein essential for regulation of photosynthetic light harvesting. Li, X., Björkman, O., Shih, C., Grossman, A. R., Rosenquist, M., Jansson, S., & Niyogi, K. K. Nature, 403(6768):391–395, January, 2000. Bandiera_abtest: a Cg_type: Nature Research Journals Number: 6768 Primary_atype: Research Publisher: Nature Publishing GroupPaper doi abstract bibtex Photosynthetic light harvesting in plants is regulated in response to changes in incident light intensity. Absorption of light that exceeds a plant's capacity for fixation of CO2 results in thermal dissipation of excitation energy in the pigment antenna of photosystem II by a poorly understood mechanism. This regulatory process, termed nonphotochemical quenching, maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. To identify specific proteins that are involved in nonphotochemical quenching, we have isolated mutants of Arabidopsis thaliana that cannot dissipate excess absorbed light energy. Here we show that the gene encoding PsbS, an intrinsic chlorophyll-binding protein of photosystem II, is necessary for nonphotochemical quenching but not for efficient light harvesting and photosynthesis. These results indicate that PsbS may be the site for nonphotochemical quenching, a finding that has implications for the functional evolution of pigment-binding proteins.
@article{li_pigment-binding_2000,
title = {A pigment-binding protein essential for regulation of photosynthetic light harvesting},
volume = {403},
copyright = {2000 Macmillan Magazines Ltd.},
issn = {1476-4687},
url = {https://www.nature.com/articles/35000131},
doi = {10.1038/35000131},
abstract = {Photosynthetic light harvesting in plants is regulated in response to changes in incident light intensity. Absorption of light that exceeds a plant's capacity for fixation of CO2 results in thermal dissipation of excitation energy in the pigment antenna of photosystem II by a poorly understood mechanism. This regulatory process, termed nonphotochemical quenching, maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. To identify specific proteins that are involved in nonphotochemical quenching, we have isolated mutants of Arabidopsis thaliana that cannot dissipate excess absorbed light energy. Here we show that the gene encoding PsbS, an intrinsic chlorophyll-binding protein of photosystem II, is necessary for nonphotochemical quenching but not for efficient light harvesting and photosynthesis. These results indicate that PsbS may be the site for nonphotochemical quenching, a finding that has implications for the functional evolution of pigment-binding proteins.},
language = {en},
number = {6768},
urldate = {2021-11-08},
journal = {Nature},
author = {Li, Xiao-Ping and Björkman, Olle and Shih, Connie and Grossman, Arthur R. and Rosenquist, Magnus and Jansson, Stefan and Niyogi, Krishna K.},
month = jan,
year = {2000},
note = {Bandiera\_abtest: a
Cg\_type: Nature Research Journals
Number: 6768
Primary\_atype: Research
Publisher: Nature Publishing Group},
keywords = {Humanities and Social Sciences, Science, multidisciplinary},
pages = {391--395},
}
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This regulatory process, termed nonphotochemical quenching, maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. To identify specific proteins that are involved in nonphotochemical quenching, we have isolated mutants of Arabidopsis thaliana that cannot dissipate excess absorbed light energy. Here we show that the gene encoding PsbS, an intrinsic chlorophyll-binding protein of photosystem II, is necessary for nonphotochemical quenching but not for efficient light harvesting and photosynthesis. These results indicate that PsbS may be the site for nonphotochemical quenching, a finding that has implications for the functional evolution of pigment-binding proteins.","language":"en","number":"6768","urldate":"2021-11-08","journal":"Nature","author":[{"propositions":[],"lastnames":["Li"],"firstnames":["Xiao-Ping"],"suffixes":[]},{"propositions":[],"lastnames":["Björkman"],"firstnames":["Olle"],"suffixes":[]},{"propositions":[],"lastnames":["Shih"],"firstnames":["Connie"],"suffixes":[]},{"propositions":[],"lastnames":["Grossman"],"firstnames":["Arthur","R."],"suffixes":[]},{"propositions":[],"lastnames":["Rosenquist"],"firstnames":["Magnus"],"suffixes":[]},{"propositions":[],"lastnames":["Jansson"],"firstnames":["Stefan"],"suffixes":[]},{"propositions":[],"lastnames":["Niyogi"],"firstnames":["Krishna","K."],"suffixes":[]}],"month":"January","year":"2000","note":"Bandiera_abtest: a Cg_type: Nature Research Journals Number: 6768 Primary_atype: Research Publisher: Nature Publishing Group","keywords":"Humanities and Social Sciences, Science, multidisciplinary","pages":"391–395","bibtex":"@article{li_pigment-binding_2000,\n\ttitle = {A pigment-binding protein essential for regulation of photosynthetic light harvesting},\n\tvolume = {403},\n\tcopyright = {2000 Macmillan Magazines Ltd.},\n\tissn = {1476-4687},\n\turl = {https://www.nature.com/articles/35000131},\n\tdoi = {10.1038/35000131},\n\tabstract = {Photosynthetic light harvesting in plants is regulated in response to changes in incident light intensity. Absorption of light that exceeds a plant's capacity for fixation of CO2 results in thermal dissipation of excitation energy in the pigment antenna of photosystem II by a poorly understood mechanism. This regulatory process, termed nonphotochemical quenching, maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. To identify specific proteins that are involved in nonphotochemical quenching, we have isolated mutants of Arabidopsis thaliana that cannot dissipate excess absorbed light energy. Here we show that the gene encoding PsbS, an intrinsic chlorophyll-binding protein of photosystem II, is necessary for nonphotochemical quenching but not for efficient light harvesting and photosynthesis. 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