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Number of results
2012 | 121 | 2 | 397-400

Article title

Spectroscopy of Photosynthetic Pigment-Protein Complex LHCII

Content

Title variants

Languages of publication

EN

Abstracts

EN
Light-harvesting pigment-protein complex of photosystem II is the most abundant membrane protein in the biosphere, comprising more than half chlorophyll molecules. The protein plays a role of photosynthetic antenna, collecting solar radiation and transferring excitations towards the reaction centers, where electric charge separation takes place. Efficient excitation energy capture and transfer requires unique organization of the complex and unique photophysical properties of the accessory pigments: chlorophylls and carotenoids. LHCII is also a place where extremely harmful singlet oxygen may be generated, under strong illumination conditions. Several physical mechanisms have been found in LHCII, operating to protect the photosynthetic apparatus against light-induced damage, including chlorophyll triplet and singlet excitations quenching by carotenoids. In this paper we discuss the results of our recent studies, carried out with the application of several molecular spectroscopy techniques (electronic absorption, fluorescence, resonance Raman and FTIR), designed to investigate molecular mechanisms responsible for regulation of excitation density in LHCII. Among the most interesting findings are the light-induced molecular configuration changes of the LHCII-bound xanthophylls, leading to conformational rearrangements of the protein. These mechanisms are discussed in terms of excessive excitation quenching in the pigment-protein complex subjected to overexcitation. Such an activity seems to represent a vital regulatory process in the photosynthetic apparatus, at the molecular level, protecting plants against photodegradation.

Keywords

EN

Year

Volume

121

Issue

2

Pages

397-400

Physical description

Dates

published
2012-02

Contributors

author
  • Department of Biophysics, Institute of Physics, Maria Curie-Skłodowska University, Lublin, Poland
author
  • Department of Biophysics, Institute of Physics, Maria Curie-Skłodowska University, Lublin, Poland
author
  • Department of Biophysics, Institute of Physics, Maria Curie-Skłodowska University, Lublin, Poland
author
  • Department of Biophysics, Institute of Physics, Maria Curie-Skłodowska University, Lublin, Poland
author
  • Centre for Commercialization of Fluorescence Technologies, University of North Texas, Health Science Center, Fort Worth, USA
author
  • Centre for Commercialization of Fluorescence Technologies, University of North Texas, Health Science Center, Fort Worth, USA

References

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-appv121n253kz
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