ATP-induced quenching of chlorophyll fluorescence in chloroplasts of higher plants. Dependence on structural properties of the membranes |
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| Authors: | C Scoufflaire E Martens R Lannoye J Barber |
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| Institution: | (1) Laboratoire de Physiologie végétale, Université Libre de Bruxelles, Avenue Paul Heger 28, 1050 Bruxelles, Beigique;(2) Department of Pure and Applied Biology, Imperial College of Science and Technology, SW7 2BB London, U.K. |
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| Abstract: | The ATP-induced quenching of chlorophyll fluorescence in chloroplasts of higher plants is shown to be inhibited when the mobility of the protein complexes into the thylakoid membranes is reduced. Its occurrence also requires the presence of LHC complexes and the ability of the membranes to unstack.These observations, in addition to a slight increase of charge density of the surface-as indicated by 9-aminoacridine fluorescence and high salt-induced chlorophyll fluorescence studies-and partial unstacking of the membranes-as monitored by digitonin method and 540 nm light scattering changes-after phosphorylation, suggest that the ATP-induced quenching of chlorophyll fluorescence could reflect some lateral redistribution of membrane proteins in the lipid matrix of the thylakoids.Abbreviations ATP
adenosine triphosphate
- 9-AA
9-aminoacridine
- Chl
chlorophyll
- EDTA
ethylenediaminetetraacetate
- GDA
glutaraldehyde
- Hepes
N-2-hydroxyethylpiperazine-N -2-ethane-sulphonic acid
- LHC
light-harvesting chlorophyll a/b complex PS photosystem |
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| Keywords: | Chlorophyll fluorescence Light-harvesting chlorophyll protein complex Protein diffusion Protein phosphorylation Thylakoid membranes |
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