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Molecular basis of photoprotection and control of photosynthetic light-harvesting

Author

Listed:
  • Andrew A. Pascal

    (URA2096/CNRS and DBJC/CEA, CEA-Saclay)

  • Zhenfeng Liu

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Koen Broess

    (Wageningen University)

  • Bart van Oort

    (Wageningen University)

  • Herbert van Amerongen

    (Wageningen University)

  • Chao Wang

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Peter Horton

    (University of Sheffield)

  • Bruno Robert

    (URA2096/CNRS and DBJC/CEA, CEA-Saclay)

  • Wenrui Chang

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Alexander Ruban

    (University of Sheffield)

Abstract

A trick with the light A green plant can photosynthesize in shade pretty effectively, by collecting as much light as possible via an antenna made up of chlorophyll attached to a matrix of specialized proteins. In full sunlight though, the problem is rather different. When there is too much light it becomes necessary to ‘lose’ some of the Sun's energy in order to avoid bleaching damage. Little is known about the mechanism of the safety valve involved, but now it has been established that the atomic structure of the major plant light-harvesting antenna protein, published in Nature recently (428, 287–292; 2004), was in fact that of the molecule in a dissipative energy-wasting state. Armed with that knowledge and a spectroscopic analysis of the protein crystal, it is now possible to see how this protein, LHCII, changes the configuration of its pigment array in response to changes in light intensity. This has implications not just for improving the resistance of crops to stress but also for design of novel nano-optical devices.

Suggested Citation

  • Andrew A. Pascal & Zhenfeng Liu & Koen Broess & Bart van Oort & Herbert van Amerongen & Chao Wang & Peter Horton & Bruno Robert & Wenrui Chang & Alexander Ruban, 2005. "Molecular basis of photoprotection and control of photosynthetic light-harvesting," Nature, Nature, vol. 436(7047), pages 134-137, July.
  • Handle: RePEc:nat:nature:v:436:y:2005:i:7047:d:10.1038_nature03795
    DOI: 10.1038/nature03795
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    Cited by:

    1. Edoardo Cignoni & Margherita Lapillo & Lorenzo Cupellini & Silvia Acosta-Gutiérrez & Francesco Luigi Gervasio & Benedetta Mennucci, 2021. "A different perspective for nonphotochemical quenching in plant antenna complexes," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    2. Volha U. Chukhutsina & James M. Baxter & Alisia Fadini & Rhodri M. Morgan & Matthew A. Pope & Karim Maghlaoui & Christian M. Orr & Armin Wagner & Jasper J. Thor, 2022. "Light activation of Orange Carotenoid Protein reveals bicycle-pedal single-bond isomerization," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Davide Accomasso & Giacomo Londi & Lorenzo Cupellini & Benedetta Mennucci, 2024. "The nature of carotenoid S* state and its role in the nonphotochemical quenching of plants," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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