Acceptor side photoinhibition in PS II: on the possible effects of the functional integrity of the PS II donor side on photoinhibition of stable charge separation

• Published in: Photosynthesis research 1997, Vol.52 (3), p.199-213
• Main Authors: Napiwotzki, A, Bergmann, A, Decker, K, Legall, H, Eckert, H.J, Eichler, H.J, Renger, G
• Format: Article
• Language: English
• Subjects: Bacteria; chlorophyll; dark; duration; electron transfer; fluorescence; irradiation; photoinhibition; Photosynthesis; photosystem II; Spinacia oleracea; thylakoids
• ISSN: 0166-8595; 1573-5079
• DOI: 10.1023/a:1005897503276

Photoinhibition under aerobic and anaerobic conditions was analyzed in O^sub 2^-evolving and in Tris-treated PS II-membrane fragments from spinach by measuring laser-flash-induced absorption changes at 826 nm reflecting the transient P680^sup +^ formation and the chlorophyll fluorescence lifetime. It was found that anaerobic photoinhibitory treatment leads in both types of samples to the appearence of two long-lived fluorescence components with lifetimes of 7 ns and 16 ns, respectively. The extent of these fluorescence kinetics depends on the state of the reaction center (open/closed) during the fluorescence measurements: it is drastically higher in the closed state. It is concluded that this long-lived fluorescence is mainly emitted from modified reaction centers with singly reduced Q^sub A^(Q^sub A^^sup -^). This suggests that the observation of long-lived fluorescence components cannot necessarily be taken as an indicator for reaction centers with missing or doubly reduced and protonated Q^sub A^ (Q^sub A^H^sub 2^). Time-resolved measurements of 826 nm absorption changes show that the rate of photoinhibition of the stable charge separation (P680^sup *^Q^sub A^ [arrow right] P680^sup +^Q^sub A^^sup -^), is nearly the same in O^sub 2^-evolving and in Tris-treated PS II-membrane fragments. This finding is difficult to understand within the framework of the Q^sub A^H^sub 2^-mechanism for photoinhibition of stable charge separation because in that case the rate of photoinhibition should strongly depend on the functional integrity of the donor side of PS II. Based on the results of this study it is inferred, that several processes contribute to photoinhibition within the PS II reaction center and that a mechanism which comprises double reduction and protonation of Q^sub A^ leading to Q^sub A^H^sub 2^ formation is only of marginal - if any - relevance for photoinhibition of PS II under both, aerobic and anaerobic, conditions.[PUBLICATION ABSTRACT]