Partial disintegration and reconstitution of the photosynthetic oxygen evolution system. Binding of 24 kilodalton and 18 kilodalton polypeptides

Mitsue Miyao, Norio Murata

Research output: Contribution to journalArticlepeer-review

151 Citations (Scopus)

Abstract

Treatment with 1 M NaCl almost totally removed two polypeptides of 24 and 18 kDa from the Photosystem II particles of spinach chloroplasts and reduced the oxygen-evolution activity by about half. Both polypeptides were able to rebind to the NaCl-treated particles in a low-salt medium. The rebinding of the 24 kDa polypeptide showed a saturation curve whose maximum level was close to that naturally occurring in the untreated particles. In parallel with the amount of rebound 24 kDa polypeptide, the oxygen-evolution activity was recovered. The 18 kDa polypeptide bound to the NaCl-treated particles without saturation. When the 18 kDa polypeptide was added to the particles previously treated with NaCl and then supplemented with a saturating amount of 24 kDa polypeptide, there appeared, in addition to the binding without saturation, another binding of the 18 kDa polypeptide with saturation to a maximum level close to that naturally occurring in the untreated particles. The 18 kDa polypeptide did not restore the oxygen-evolution activity. These findings suggest that there are specific binding sites; one for the 24 kDa polypeptide located on the Photosystem II particles, and the other for the 18 kDa polypeptide on the 24 kDa polypeptide.

Original languageEnglish
Pages (from-to)87-93
Number of pages7
JournalBBA - Bioenergetics
Volume725
Issue number1
DOIs
Publication statusPublished - 1983 Oct 31
Externally publishedYes

Keywords

  • (Spinach chloroplast)
  • Oxygen evolution
  • Photosynthesis
  • Photosystem II
  • Protein binding

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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