Structural and Functional Properties of the Isolated Photosystem Two Reaction Centre

  • J. Barber
  • D. J. Chapman
  • K. Gounaris
  • J. B. Marder
  • A. Telfer
Part of the NATO ASI Series book series (NSSA, volume 168)


The sequencing of the genes for the L and M subunits of the purple bacterial reaction centre and the D1 and D2 polypeptides of photosystem two (PS2) revealed striking homologies in localized areas (1,2). The likely meaning of these homologies emerged from the X-ray crystallography work of Deisenhofer et al (3) using crystals of the isolated reaction centre of Rhodopseudomonas viridis. Such a comparison indicated that like the L and M polypeptides, the D1 and D2 polypeptides probably form the heart of the PS2 reaction centre (4–6). This prediction was supported by work of Nanba and Satoh (7) who isolated a chlorophyll binding complex from spinach chloroplasts consisting only of the D1, D2 and cytochrome b559 polypeptides which were able to catalyse photoreactions indicative of the PS2 reaction centre. Using pea rather than spinach, we also isolated a D1/D2/cyt b559 complex which we have subjected to detailed structural and functional analysis. Here we summarise our findings.


Reaction Centre Chlorophyll Fluorescence Cytochrome B559 Photosynthetic Reaction Centre Reaction Centre Complex 
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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • J. Barber
    • 1
  • D. J. Chapman
    • 1
  • K. Gounaris
    • 1
  • J. B. Marder
    • 1
  • A. Telfer
    • 1
  1. 1.AFRC Photosynthesis Research Group, Department of Pure & Applied Biology, Technology & MedicineImperial College of ScienceLondonUK

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