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  Crystal structure of plant light-harvesting complex shows the active, energy-transmitting state

Barros, T., Royant, A., Standfuss, J., Dreuw, A., & Kühlbrandt, W. (2009). Crystal structure of plant light-harvesting complex shows the active, energy-transmitting state. The EMBO Journal, 28(3), 298-306. doi:10.1038/emboj.2008.276.

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 Creators:
Barros, Tiago1, Author           
Royant, Antoine2, 3, Author
Standfuss, Jörg1, Author           
Dreuw, Andreas4, Author
Kühlbrandt, Werner1, Author                 
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Laboratoire de Cristallogenèse et Cristallographie des Protéines, Institut de Biologie Structurale J‐P Ebel, UMR 5075 CNRS–CEA–UJF, Grenoble, France, ou_persistent22              
3European Synchrotron Radiation Facility, Grenoble, France, ou_persistent22              
4Institute for Physical and Theoretical Chemistry, Johann Wolfgang Goethe‐University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: chlorophyll; fluorescence; light harvesting; non-photochemical quenching; photosynthesis
 Abstract: Plants dissipate excess excitation energy as heat by non‐photochemical quenching (NPQ). NPQ has been thought to resemble in vitro aggregation quenching of the major antenna complex, light harvesting complex of photosystem II (LHC‐II). Both processes are widely believed to involve a conformational change that creates a quenching centre of two neighbouring pigments within the complex. Using recombinant LHC‐II lacking the pigments implicated in quenching, we show that they have no particular role. Single crystals of LHC‐II emit strong, orientation‐dependent fluorescence with an emission maximum at 680 nm. The average lifetime of the main 680 nm crystal emission at 100 K is 1.31 ns, but only 0.39 ns for LHC‐II aggregates under identical conditions. The strong emission and comparatively long fluorescence lifetimes of single LHC‐II crystals indicate that the complex is unquenched, and that therefore the crystal structure shows the active, energy‐transmitting state of LHC‐II. We conclude that quenching of excitation energy in the light‐harvesting antenna is due to the molecular interaction with external pigments in vitro or other pigment–protein complexes such as PsbS in vivo, and does not require a conformational change within the complex.

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Language(s): eng - English
 Dates: 2008-08-062008-12-032009-01-082009-02-04
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/emboj.2008.276
 Degree: -

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Title: The EMBO Journal
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 28 (3) Sequence Number: - Start / End Page: 298 - 306 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1