Kinetic Absorption Spectroscopy Provides Evidence for the Function of Z in (D1,D2) Photosystem-II Reaction Centers

  • P. Mathis
  • K. Satoh
  • Ö. Hansson


In Photosystem-II (PS-II), light excitation induces the oxidation of the primary donor P-680, and the reduction of the primary acceptor, a pheophytin I. After a short flash, QA is reduced by l in less than one nanosecond and the reduction of P-680+ by the secondary donor Z takes times which vary from the 50 ns domain, under physiological conditions, to the 5–50 µs domain when oxygen evolution is inhibited. A PS-II reaction center complex has been recently isolated (1). It contains two polypeptides named D1 and D2 which hold the primary photochemical partners P-680 and I, and cytochrome b559, but QA is absent. According to recent results obtained by site-directed mutagenesis (2,3) and by specific iodination (4), Z is one of the tyrosines (Tyr-161) of the polypeptide D1. Thus Z should be present in purified (D1,D2 PS-II complexes. There is, however, no firm functional evidence for that presence. EPR measurements following illumination at low temperature, led to propose that a donor to P-680+ was operating, but its chemical identification with Z could not be obtained (5,6).


Fast Phase Reaction Center Complex Microsecond Range Short Flash Reaction Center Core 
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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • P. Mathis
    • 1
  • K. Satoh
    • 2
  • Ö. Hansson
    • 3
  1. 1.Département de Biologie, SBPhCEN SACLAYGif-sur-Yvette CedexFrance
  2. 2.Biology DepartmentOkayama UniversityOkayama 700Japan
  3. 3.Department of Biochemistry and BiophysicsUniversity of Göteborg and Chalmers Institute of TechnologyGöteborgSweden

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