ISSN:
1573-5079
Schlagwort(e):
Photoinhibition
;
Photosystem II
;
quinone-iron complex
;
electron paramagnetic resonance (EPR)
;
thermoluminescence (TL)
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
Abstract Photosystem II particles were exposed to 800 W m−2 white light at 20 °C under anoxic conditions. The Fo level of fluorescence was considerably enhanced indicating formation of stable-reduced forms of the primary quinone electron acceptor, QA. The Fm level of fluorescence declined only a little. The g=1.9 and g=1.82 EPR forms characteristic of the bicarbonate-bound and bicarbonate-depleted semiquinone-iron complex, QA −Fe2+, respectively, exhibited differential sensitivity against photoinhibition. The large g=1.9 signal was rapidly diminished but the small g=1.82 signal decreased more slowly. The S2-state multiline signal, the oxygen evolution and photooxidation of the high potential form of cytochrome b-559 were inhibited approximately with the same kinetics as the g=1.9 signal. The low potential form of oxidized cytochrome b-559 and Signal IIslow arising from TyrD + decreased considerably slower than the g=1.9 semiquinone-iron signal. The high potential form of oxidized cytochrome b-559 was diminished faster than the low potential form. Photoinhibition of the g=1.9 and g=1.82 forms of QA was accompanied with the appearance and gradual saturation of the spin-polarized triplet signal of P 680. The amplitude of the radical signal from photoreducible pheophytin remained constant during the 3 hour illumination period. In the thermoluminescence glow curves of particles the Q band (S2QA − charge recombination) was almost completely abolished. To the contrary, the C band (TyrD +QA − charge recombination) increased a little upon illumination. The EPR and thermoluminescence observations suggest that the Photosystem II reaction centers can be classified into two groups with different susceptibility against photoinhibition.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00020433
Permalink
