Mechanism of the Light State Transition in Porphyridium cruentum

Biggins, John; Campbell, Christine L.; Creswell, L. L.; Wood, Elizabeth

doi:10.1007/978-94-017-4973-2_69

Cited by 9 publications

(2 citation statements)

References 6 publications

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“…Fork and Satoh (1983), Satoh and Fork (1983a), Biggins (1983) and Biggins et al (1984a), demonstrated a 30-100% increase in turnover of PSI upon transition of cells to state 2 at room temperature. Fork and Satoh (1983), Satoh and Fork (1983a), Biggins (1983) and Biggins et al (1984a), demonstrated a 30-100% increase in turnover of PSI upon transition of cells to state 2 at room temperature.…”

Section: Electron Transportmentioning

confidence: 99%

“…The transition to state 1 requires coupled PSI electron transport (Fork and Satoh 1983, Satoh and Fork 1983b, Biggins et al 1984a, and full conversion requires only 15 turnovers of RC1 corresponding to the formation of the transmembrane proton gradient (Graan andOrt 1982, Biggins andBruce 1985a). The transition to state 1 requires coupled PSI electron transport (Fork and Satoh 1983, Satoh and Fork 1983b, Biggins et al 1984a, and full conversion requires only 15 turnovers of RC1 corresponding to the formation of the transmembrane proton gradient (Graan andOrt 1982, Biggins andBruce 1985a).…”

Section: Evaluation Of Biochemical Parametersmentioning

confidence: 99%

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Regulation of excitation energy transfer in organisms containing phycobilins

1989

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The mechanism of excitation energy redistribution (state transition) in organisms containing phycobilins is reviewed. Recent measurements using time-resolved fluorescence spectroscopy in the picosecond range confirm that the state transition in cyanobacteria and red algae is controlled by changes in the kinetics of energy transfer from PS 2 to PS 1 (spillover) rather than by physical dislocation of the phycobilisome and reassociation between the two photosystems (mobile antenna model). Contrary to the analogous situation in higher plants, there is no compelling evidence for the involvement of a protein phosphorylation event in the rapid time range of the state transition, but a variety of data indicate that a membrane conformational change occurs that might change the relative distance between, and/or orientation of the two photosystems within the thylakoid. The state transition is most probably initiated by the redox state of the intersystem electron transport chain, and the conversion to state 1 is driven by coupled PS1 cyclic electron transport. The cryptomonads also undergo wavelength dependent changes in excitation energy distribution by a mechanism very similar to that observed in the red algae and cyanobacteria. However, the changes in energy distribution in this group are most likely related to a photoprotection mechanism for PS2 rather than to a state transition.

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