Visualizing the mobility and distribution of chlorophyll proteins in higher plant thylakoid membranes: effects of photoinhibition and protein phosphorylation
β Scribed by Tomasz K. Goral; Matthew P. Johnson; Anthony P.R. Brain; Helmut Kirchhoff; Alexander V. Ruban; Conrad W. Mullineaux
- Book ID
- 110095996
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 785 KB
- Volume
- 62
- Category
- Article
- ISSN
- 0960-7412
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π SIMILAR VOLUMES
When the capacity of leaves for orderly dissipation of excitation energy in photosynthesis is exceeded, one mechanism by which the excess energy appears to be dissipated is through a nonradiative decay process. This process is observed as a reversible quenching of chlorophyll fluorescence emission (
Thylakoid membranes retaining a high capacity to phosphorylate the D 1 protein of photosystem II but free from contamination by exogenous proteases have been prepared. Almost all the DI protein in this preparation is unphosphorylated, but it is almost completely phosphorylated by illumination in the
The phosphorylation of proteins in the synaptic plasma membrane is a rather slow reaction taking several minutes to saturate all the phosphate acceptor sites. (The time for half the protein bound phosphate groups to turnover is about 1 min). A divalent cation is needed as a cofactor for the reaction