Reduced content of the quinone acceptor QA in photosystem II complexes isolated from thylakoid membranes after prolonged photoinhibition under anaerobic conditions.
The plastoquinone content of photosystem II complexes isolated from spinach photosystem II-enriched membranes subjected to strong photoinhibitory illumination under anaerobic conditions was determined by HPLC. A pronounced decrease of the plastoquinone content was found in the photoinactivated complexes. These results corroborate earlier models in which photoinhibitory illumination is suggested to eventually lead to release of doubly reduced and protonated QA from its site on the D2-protein.
Koivuniemi
A
A
Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.
Swiezewska
E
E
Aro
E M
EM
Styring
S
S
Andersson
B
B
D001665:Binding Sites; D004579:Electron Transport; D007425:Intracellular Membranes / Q000378:metabolism*; D008027:Light; D010100:Oxygen / Q000378:metabolism*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D010971:Plastoquinone / Q000378:metabolism*
D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010971:Plastoquinone; D010100:Oxygen