Light-induced gradual activation of photosystem II in dark-grown Norway spruce seedlings
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
26901522
DOI
10.1016/j.bbabio.2016.02.009
PII: S0005-2728(16)30028-7
Knihovny.cz E-zdroje
- Klíčová slova
- Chlorophyll biosynthesis, Chlorophyll fluorescence, DPOR, Norway spruce, Oxygen evolving complex, PSII supercomplex,
- MeSH
- chlorofyl a MeSH
- chlorofyl chemie metabolismus MeSH
- fotosyntéza účinky záření MeSH
- fotosystém I - proteinový komplex metabolismus MeSH
- fotosystém II - proteinový komplex metabolismus MeSH
- kotyledon růst a vývoj metabolismus účinky záření MeSH
- kyslík metabolismus MeSH
- luminiscenční měření metody MeSH
- rostlinné proteiny metabolismus MeSH
- semenáček růst a vývoj metabolismus účinky záření MeSH
- smrk růst a vývoj metabolismus účinky záření MeSH
- světlo * MeSH
- teplota MeSH
- tma * MeSH
- transport elektronů účinky záření MeSH
- tylakoidy metabolismus účinky záření MeSH
- western blotting MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- chlorofyl a MeSH
- chlorofyl MeSH
- fotosystém I - proteinový komplex MeSH
- fotosystém II - proteinový komplex MeSH
- kyslík MeSH
- rostlinné proteiny MeSH
Gymnosperms, unlike angiosperms, are able to synthesize chlorophyll and form photosystems in complete darkness. Photosystem I (PSI) formed under such conditions is fully active, but photosystem II (PSII) is present in its latent form with inactive oxygen evolving complex (OEC). In this work we have studied light-induced gradual changes in PSII function in dark-grown cotyledons of Norway spruce (Picea abies) via the measurement of chlorophyll a fluorescence rise, absorption changes at 830 nm, thermoluminescence glow curves (TL) and protein analysis. The results indicate that in dark-grown cotyledons, alternative reductants were able to act as electron donors to PSII with inactive OEC. Illumination of cotyledons for 5 min led to partial activation of PSII, which was accompanied by detectable oxygen evolution, but still a substantial number of PSII centers remained in the so called PSII-Q(B)-non-reducing form. Interestingly, even 24 h long illumination was not sufficient for the full activation of PSII centers. This was evidenced by a weak attachment of PsbP protein and the absence of PsbQ protein in PSII particles, the absence of PSII supercomplexes, the suboptimal maximum yield of PSII photochemistry, the presence of C band in TL curve and also the presence of up-shifted Q band in TL in DCMU-treated cotyledons. This slow light-induced activation of PSII in dark-grown cotyledons could contribute to the prevention of PSII overexcitation before the light-induced increase in PSI/PSII ratio allows effective operation of linear electron flow.
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