Fluorescence Properties of Isolated Chlorophyll-Protein Complexes
The chlorophyll-protein subunits of Photosystem I and II have been isolated and their fluorescence maxima established, due to the combined effort of many workers. The available data are reviewed. They characterize the individual chlorophyll-protein complexes and add to the understanding of fluorescence emitted by intact thylakoids.
Various lipids are able to incorporate separated chlorophyll-protein complexes into proteolipid particles. Fluorescence emission spectra of the separated complexes and of the proteolipid particles are used to reveal interruption and restoration, respectively, of energy transfer between the different chlorophyll-protein complexes.
The pigments of the light-harvesting Chl-a/b-protein complex (LHC-II) are stable under strong white light, but they are readily photo-oxidised in the presence of limonene or Triton X-100. The fluorescence excitation spectrum of LHC-II reveals differences in the mode of action of limonene and Triton X-100. Evidence for the protective role of LHC-II apoprotein is obtained from these and other experiments.
Key wordsChlorophyll-protein complexes Photosystem I Photosystem II Chlorophyll-proteolipid particles Light-harvesting chlorophyll-a/b-protein complex II (LHC-II) Fluorescence emission Fluorescence excitation Energy transfer Limonene Photooxidation
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