The Physiological Significance of Thylakoid Membrane Protein Phosphorylation

@inproceedings{Melis1987ThePS,
  title={The Physiological Significance of Thylakoid Membrane Protein Phosphorylation},
  author={Anastasios Melis and Xin Deng},
  year={1987},
  url={https://api.semanticscholar.org/CorpusID:101025295}
}
The energetic coupling of phospho-LHC II with PSI, however, is currently a controversial issue with more research required to provide unambiguous answers.
1 Citation

Post-transcriptional control of plastid mRNA accumulation during adaptation of chloroplasts to different light quality environments.

Post-transcriptional mechanisms are primarily responsible for the control of differential chloroplast mRNA accumulation in light quality adaptations of spinach seedlings to yellow and red light.

Phosphorylation of chloroplast membrane polypeptides

Protein phosphorylation is a reversible, energy-dependent membrane modification, but it differs from the other changes in that it takes the form of a specific chemical reaction involving certain identifiable chloroplast membrane polypeptides.

Chloroplast phosphoproteins: regulation of excitation energy transfer by phosphorylation of thylakoid membrane polypeptides.

It is concluded that a membrane-bound protein kinase can phosphorylate surface-exposed segments of the light-harvesting pigment-protein complex, altering the properties of its interaction with the two photosystems such that the distribution of absorbed excitation energy increasingly favors photosystem I.

CHLOROPLAST MEMBRANE PROTEIN PHOSPHORYLATION

A hypothesis explaining the biochemical basis of state changes was recently presented and LHC-I1 phosphorylation was suggested to cause State I-State I1 transitions, and a summary of the evidence which has accumulated is presented.

Photosystem electron-transport capacity and light-harvesting antenna size in maize chloroplasts.

The PSII/PSI electron-transport capacity ratio (C) in maize chloroplasts is estimated, indicating that, under green actinic excitation when Chl a and Chl b molecules absorb nearly equal amounts of excitation, PSII has a capacity to turn over electrons faster than PSI.