Photosystem II — Details of Cofactor-Protein Interactions in the Light of the 3 Å Resolution Crystal Structure

  • Matthias Broser
  • Albert Guskov
  • Jan Kern
  • Junko Yano
  • Vittal Yachandra
  • Bernhard Loll
  • Jacek Biesiadka
  • Wolfram Saenger
  • Athina Zouni

Abstract

The large membrane intrinsic protein complex Photosytem II (PSII) catalyses light-driven charge separation accompanied by the oxidation of water during oxygenic photosynthesis. In this contribution we will discuss the recent X-ray crystallographic structural model at 3 Å resolution (Loll et al. 2005) in relation to various spectroscopic and biochemical data. Special emphasis will be given on: (A) the quinone binding pockets, the proposed diffusion pathway of quinones into the QB binding site and the possible binding of additional quinones within the complex; (B) the catalytic center for light-induced water oxidation (the Mn4-Ca cluster). The arrangement of metal cations in the cluster, their coordination and protein surroundings are discussed with regard to spectroscopic and mutagenesis studies. Limitations of the presently available structural data are pointed out and the very recent results of X-ray spectroscopy (XANES and EXAFS) on PSII single crystals (Yano et al. 2006) are described in comparison with the X-ray crystallographic model of the water oxidizing complex.

Keywords

Photosystem II structure plastoquinone manganese cluster EXAFS 

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References

  1. Debus RJ (2005) In: Wydrzynski T, Satoh K (eds) Photosystem II: The Light Driven Water:Plastoquinone Oxidoreductase. Springer, Dordrecht, The Netherlands.Google Scholar
  2. Ferreira KN, Iverson TN, Maghlaoui K, Barber J, Iwata S (2004) Architecture of the photosynthetic oxygen-evolving center. Science 303:1831-1838.PubMedCrossRefGoogle Scholar
  3. Loll B, Kern J, Saenger W, Zouni A, Biesiadka J (2005) Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 438:1040-1044.PubMedCrossRefGoogle Scholar
  4. Loll B, Kern J, Saenger W, Zouni A, Biesiadka J (2007) Lipids in Photosystem II: Interactions with protein and cofactors. Biochim Biophys Acta 1767:509-519.PubMedCrossRefGoogle Scholar
  5. Kern J, Loll B, Lüneberg C, DiFiore D, Biesiadka J, Irrgang KD, Zouni A (2005) Purification, characterisation and crystallisation of photosystem II from Thermosynechococcus elongatus cultivated in a new type of photobioreactor. Biochim Biophys Acta 1706:147-157.PubMedCrossRefGoogle Scholar
  6. Kern J, Biesiadka J, Loll B, Saenger W, Zouni A (2007) Structure of the Mn(4)-Ca cluster as derived from X-ray diffraction. Photosynth Res 92:389-405.PubMedCrossRefGoogle Scholar
  7. Krivanek R, Kern J, Zouni A, Dau H, Haumann M (2007) Spare quinones in the QB cavity of crystallized photosystem II from Thermosynechococcus elongatus. Biochim Biophys Acta 1767:520-527.PubMedCrossRefGoogle Scholar
  8. Yano J, Kern J, Irrgang KD, Latimer MJ, Bergmann U, Glatzel P, Pushkar Y, Biesiadka J, Loll B, Sauer K, Messinger J, Zouni A, Yachandra VK (2005) X-ray damage to the Mn4Ca complex in single crystals of photosystem II: A case study for metalloprotein crystallography. Proc Natl Acad Sci USA 102:12047-12052.PubMedCrossRefGoogle Scholar
  9. Yano J, Kern J, Sauer K, Latimer MJ, Pushkar Y, Biesiadka J, Loll B, Saenger W, Messinger J, Zouni A, Yachandra VK (2006) Where water is oxidized to dioxygen: Structure of the photosynthetic Mn4Ca cluster. Science 314:821-825.PubMedCrossRefGoogle Scholar
  10. Zimmermann K, Heck M, Frank J, Kern J, Vass I, Zouni A (2006) Herbicide binding and thermal stability of photosystem II isolated from Thermosynechococcus elongatus. Biochim Biophys Acta 1757:106-114.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science + Business Media, B.V. 2008

Authors and Affiliations

  • Matthias Broser
    • 1
  • Albert Guskov
    • 2
  • Jan Kern
    • 1
  • Junko Yano
    • 3
  • Vittal Yachandra
    • 3
  • Bernhard Loll
    • 2
  • Jacek Biesiadka
    • 2
  • Wolfram Saenger
    • 2
  • Athina Zouni
    • 1
  1. 1.Max-Volmer-LaboratoriumTechnical University BerlinBerlinGermany
  2. 2.Institute for CristallographyFree University BerlinBerlinGermany
  3. 3.Melvin Calvin LaboratoryPhysical Biosciences Division, Lawrence Berkeley National LaboratoryBerkeleyUSA

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