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Correlation of iron content, spectral forms of chlorophyll and chlorophyll‐proteins in iron deficient cucumber ( Cucumis sativus )
Author(s) -
Fodor Ferenc,
Böddi Béla,
Sárvári Éva,
Záray Gyula,
Cseh Edit,
Láng Ferenc
Publication year - 1995
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1995.tb05127.x
Subject(s) - photosystem ii , cucumis , photosynthesis , chloroplast , photosystem i , chlorophyll , iron deficiency , chemistry , chlorophyll a , fluorescence , chlorophyll fluorescence , biology , botany , biophysics , biochemistry , medicine , physics , quantum mechanics , gene , anemia
Leaves and chloroplast suspensions of severely and slightly iron deficient cucumber ( Cucumis sativus L.) plants were characterized by low‐temperature fluorescence emission spectroscopy and Deriphat polyacrylamide gel electrophoresis. The emission spectra of the chloroplast suspensions were resolved into Gaussian components and those changes induced by iron deficiency were related to the variations in the chlorophyll‐protein pattern. The symptoms described with these methods were also correlated with the iron content of the leaves. It was concluded that the lack of physiologically active iron caused a relative decrease of photosystem I (PSI) and light harvesting complex I (LHCI), together with the long wavelength fluorescence, especially the 740 nm Gaussian component, and. to a much lesser extent, of the photosystem II (PSII) core complexes (relative increase of 685, 695 nm components). However, the relative decrease in the amount of light harvesting complex II (LHCII) was followed by a relative increase in its fluorescence band at 680 nm, showing that energy transfer from LHCII to core complex II (CCII) was partly disturbed. Thus iron deficiency affected the photosynthetic apparatus in a complex way: it decreased the synthesis of chlorophylls (Chls) and influenced the expression and assembly of Chl‐binding proteins.