Light harvesting in photosystem II View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-04-18

AUTHORS

Herbert van Amerongen, Roberta Croce

ABSTRACT

Water oxidation in photosynthesis takes place in photosystem II (PSII). This photosystem is built around a reaction center (RC) where sunlight-induced charge separation occurs. This RC consists of various polypeptides that bind only a few chromophores or pigments, next to several other cofactors. It can handle far more photons than the ones absorbed by its own pigments and therefore, additional excitations are provided by the surrounding light-harvesting complexes or antennae. The RC is located in the PSII core that also contains the inner light-harvesting complexes CP43 and CP47, harboring 13 and 16 chlorophyll pigments, respectively. The core is surrounded by outer light-harvesting complexes (Lhcs), together forming the so-called supercomplexes, at least in plants. These PSII supercomplexes are complemented by some “extra” Lhcs, but their exact location in the thylakoid membrane is unknown. The whole system consists of many subunits and appears to be modular, i.e., both its composition and organization depend on environmental conditions, especially on the quality and intensity of the light. In this review, we will provide a short overview of the relation between the structure and organization of pigment-protein complexes in PSII, ranging from individual complexes to entire membranes and experimental and theoretical results on excitation energy transfer and charge separation. It will become clear that time-resolved fluorescence data can provide invaluable information about the organization and functioning of thylakoid membranes. At the end, an overview will be given of unanswered questions that should be addressed in the near future. More... »

PAGES

251-263

References to SciGraph publications

  • 2004-12. Structure, function and assembly of Photosystem II and its light-harvesting proteins in PHOTOSYNTHESIS RESEARCH
  • 2008-10. Dynamic flexibility in the structure and function of photosystem II in higher plant thylakoid membranes: the grana enigma in PHOTOSYNTHESIS RESEARCH
  • 2009-02-15. Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2001-09. Acclimation of Arabidopsis thaliana to the light environment: the existence of separate low light and high light responses in PLANTA
  • 2008-10-01. Photosystem II: The machinery of photosynthetic water splitting in PHOTOSYNTHESIS RESEARCH
  • 2008-04-29. Toward understanding molecular mechanisms of light harvesting and charge separation in photosystem II in PHOTOSYNTHESIS RESEARCH
  • 2011-02-06. Structural insights into energy regulation of light-harvesting complex CP29 from spinach in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1999-05. Similarity between electron donor side reactions in the solubilized Photosystem II–LHC II supercomplex and Photosystem-II-containing membranes in PHOTOSYNTHESIS RESEARCH
  • 2011-04-17. Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å in NATURE
  • 2003. Light-Harvesting in Photosystem II in LIGHT-HARVESTING ANTENNAS IN PHOTOSYNTHESIS
  • 1991-06. Microwave and optical spectroscopy of carotenoid triplets in light-harvesting complex LHC II of spinach by absorbance-detected magnetic resonance in APPLIED MAGNETIC RESONANCE
  • 2004-03. Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution in NATURE
  • 2006-05-12. A comparison of the three isoforms of the light-harvesting complex II using transient absorption and time-resolved fluorescence measurements in PHOTOSYNTHESIS RESEARCH
  • 1995-05. Sequence conservation of light-harvesting and stress-response proteins in relation to the three-dimensional molecular structure of LHCII in PHOTOSYNTHESIS RESEARCH
  • 1989-12. Photoelectric study on the kinetics of trapping and charge stabilization in oriented PS II membranes in PHOTOSYNTHESIS RESEARCH
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    URI

    http://scigraph.springernature.com/pub.10.1007/s11120-013-9824-3

    DOI

    http://dx.doi.org/10.1007/s11120-013-9824-3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1025197531

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/23595278


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