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Excitation-energy distribution in green algae. The existence of two independent light-driven control mechanisms
Authors:Michael Catt  Kaoru Saito  W.Patrick Williams
Affiliation:Department of Biophysics and Bioengineering, Chelsea College, University of London, Manresa Road, London SW3 6LX U.K.
Abstract:Three distinct states can be identified for cells of the green alga Chlorella vulgaris; State 1 and State 2 obtained by preillumination in far-red and red light, respectively, and the dark state obtained by dark-adaptation. Addition of the inhibitor DCMU to algal cells leads to an initial rapid increase in chlorophyll-a fluorescence reflecting the closure of Photosystem II traps. This, in the case of dark and state-2-adapted algae is followed by a slow light-dependent increase to a fluorescence yield typical of State-1-adapted cells. Measurements of low temperature (77 K) emission spectra indicate that the low fluorescence yields of dark and State-2-adapted algae reflect similar balances in excitation-energy distribution between the two photosystems. In both cases, the balance favours PS I and the slow fluorescence increase seen in the poisoned algae reflects a redressing of this balance in favour of PS II. The low fluorescence yield of State-2-adapted algae is thought to be associated with the phosphorylation of chlorophyll a/b light-harvesting protein (Biochim. Biophys. Acta (1983) 724, 94–103). Measurements of the uncoupler and ATPase sensitivity of the light-dependent increases seen in DCMU-poisoned cells indicate that the low fluorescence yield of dark-adapted algae is of different origin. Evidence is presented showing that the light-driven changes in excitation-energy distribution seen in green algae involve two distinct processes; a low-intensity, wavelenght-independent change reflecting simple light/dark changes and a higher intensity, wavelength-dependent change reflecting State 1/State 2 adaptation. The former changes appear to be associated with changes in the local ionic environment within the algal chloroplast, whilst the latter appear to reflect changes in the phosphorylation state of chlorophyll a/b light-harvesting protein.
Keywords:Light-harvesting complex  Chlorophyll fluorescence  Excitation-energy distribution  Protein phosphorylation  (C. vulgaris)  PS I  Photosystem I  PS II  Photosystem II  LHC-II  chlorophyll a/b light-harvesting protein  DCMU  3-(3′,4′ dichlorophenyl)-1,1′-dimethylurea  CCCP  DCCD  To whom correspondence should be addressed.
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