Spectral characterization of chlorophyll fluorescence in barley leaves during linear heating. Analysis of high-temperature fluorescence rise around 60 degrees C
Jazyk angličtina Země Švýcarsko Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
11332877
DOI
10.1016/s1011-1344(00)00146-9
PII: S1011-1344(00)00146-9
Knihovny.cz E-zdroje
- MeSH
- chlorofyl a MeSH
- chlorofyl metabolismus MeSH
- fluorescence MeSH
- fluorescenční spektrometrie metody MeSH
- fotosyntetické reakční centrum - proteinové komplexy metabolismus MeSH
- ječmen (rod) metabolismus MeSH
- listy rostlin metabolismus MeSH
- světlosběrné proteinové komplexy MeSH
- vytápění * MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- chlorofyl a MeSH
- chlorofyl MeSH
- chlorophyll b MeSH Prohlížeč
- fotosyntetické reakční centrum - proteinové komplexy MeSH
- světlosběrné proteinové komplexy MeSH
The spectral characteristics of chlorophyll fluorescence and absorption during linear heating of barley leaves within the range 25-75 degreesC (fluorescence temperature curve, FTC) were studied. Leaves with various content of light harvesting complexes (green, Chl b-less chlorina f2 and intermittent light grown) revealing different types of FTC were used. Differential absorption, emission and excitation spectra documented four characteristic phases of the FTC. The initial two FTC phases (a rise in the 46-49 degreesC region and a subsequent decrease to about 55 degreesC) mostly reflected changes in the fluorescence quantum yield peaking at about 685 nm. A steep second fluorescence rise at 55-61 degreesC was found to originate from a short-wavelength Chl a spectral form (emission maximum at 675 nm) causing a gradual blue shift of the emission spectra. In this temperature range, a clear correspondence of the blue shift in the emission and absorption spectra was found. We suggest that the second fluorescence rise in FTC reflects a weakening of the Chl a-protein interaction in the thylakoid membrane.
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