Effect of the 33-kDa protein on the S-state transitions in photosynthetic oxygen evolution

Mitsue Miyao, Norio Murata, Jean Lavorel, Brigitta Maison-Peteri, Alain Boussac, Anne Lise Etienne

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96 Citations (Scopus)


The effect of the extrinsic 33-kDa protein on the photosynthetic oxygen evolution was studied by comparing spinach Photosystem II particles depleted of the 33-kDa protein with those reconstituted with the protein. The light-intensity dependence of the oxygen-evolution activity under continuous illumination suggests that a dark step, but not a light step, in the oxygen-evolving reaction is accelerated by the 33-kDa protein. Consistently, the pattern of oxygen yield with a series of short saturating flashes, which showed a maximum on the third flash and a damped oscillation with a period of 4, was not much affected by the removal and rebinding of the 33-kDa protein, when the dark interval between the flashes was long enough, i.e., longer than 0.5 s. The millisecond kinetics of oxygen release after the third flash was retarded by the removal of the 33-kDa protein and stimulated by its rebinding, suggesting that the transition from S3 to S0 is accelerated by the 33-kDa protein. The stability of the S2 and S3 states in darkness was higher in the absence of the 33-kDa protein than its presence.

Original languageEnglish
Pages (from-to)151-159
Number of pages9
JournalBBA - Bioenergetics
Issue number2
Publication statusPublished - 1987 Feb 11
Externally publishedYes


  • (Spinach)
  • Oxygen evolution
  • Photosynthesis
  • Photosystem II
  • S-state transition

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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