Removal of 33 kDa extrinsic protein specifically stabilizes the S2QA- charge pair in photosystem II

Imre Vass, Taka aki Ono, Yorinao Inoue

Research output: Contribution to journalArticle

24 Citations (Scopus)


Removal of the 33 kDa extrinsic protein from photosystem (PS) II membranes resulted in markedly increased stabilization of the S2QA- charge pair as measured by thermoluminescence. The stabilization increase was specific for the S2QA- charge pair and did not require any special herbicide. The effect was fully reversed by reconstitution with the 33 kDa protein, but not at all by high concentrations of Cl-, as opposed to those effects known to be reversed by 200 mM Cl- . The data are interpreted as indicating a structural change of the donor and/or acceptor side of PS II dependent on association with the 33 kDa extrinsic protein.

Original languageEnglish
Pages (from-to)215-220
Number of pages6
JournalFEBS letters
Issue number2
Publication statusPublished - Jan 26 1987


  • 33 kDa protein
  • Oxygen evolution
  • Photosystem II
  • S state
  • Thermoluminescence

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Removal of 33 kDa extrinsic protein specifically stabilizes the S<sub>2</sub>Q<sub>A</sub><sup>-</sup> charge pair in photosystem II'. Together they form a unique fingerprint.

  • Cite this