Premium
Removal of 33 kDa extrinsic protein specifically stabilizes the S 2 Q A − charge pair in photosystem II
Author(s) -
Vass Imre,
Ono Taka-aki,
Inoue Yorinao
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81439-4
Subject(s) - photosystem ii , photosystem i , chemistry , charge (physics) , acceptor , crystallography , photosynthesis , biochemistry , physics , quantum mechanics , condensed matter physics
Removal of the 33 kDa extrinsic protein from photosystem (PS) II membranes resulted in markedly increased stabilization of the S 2 Q A − charge pair as measured by thermoluminescence. The stabilization increase was specific for the S 2 Q A − 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.