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Two-Dimensional Crystals of the CP47-D1-D2-Cytochrome b559 Complex of Photosystem II

  • E. J. Boekema
  • J. P. Dekker
  • S. D. Betts
  • C. F. Yocum

Abstract

Substantial progress has been made in understanding the structure and function of Photosystem II, both in terms of the catalytic activity and in terms of the polypeptides. Several groups have succeeded in reducing the oxygen-evolving reaction to a complex comprised of seven polypeptides, which, when supplemented with chloride and calcium, evolve oxygen at substantial rates. The complex includes six intrinsic membrane proteins, which serve the most essential photochemical and structural functions, and an extrinsic 33 kDa protein necessary for the stabilization of oxygen evolution. Recently, a smaller protein complex consisting of the D1, D2, 47 kDa and cytochrome b559 subunits was isolated in the non-ionic detergent Dodecylmaltoside (1,2).

Keywords

Substantial Rate High Salt Condition Taurine Concentration Intrinsic Membrane Protein Crystalline Array 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • E. J. Boekema
    • 1
  • J. P. Dekker
    • 2
  • S. D. Betts
    • 2
  • C. F. Yocum
    • 2
  1. 1.Dept. of BiochemistryUniversity of GroningenGroningenThe Netherlands
  2. 2.Dept. of BiologyThe University of MichiganAnn ArborUSA

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