Stability of water-soluble chlorophyll protein (WSCP) depends on phytyl conformation

Daniel Palm, Alessandro Agostini, Anne-Christin Pohland, Mara Werwie, Elmar Jaenicke & Harald Paulsen
Water-soluble chlorophyll proteins (WSCP) from Brassicaceae form homotetrameric chlorophyll (Chl)–protein complexes binding one Chl per apoprotein and no carotenoids. Despite the lack of photoprotecting photoprotecting pigments, the complex-bound Chls displays a remarkable stability toward photodynamic photodynamic damage. On the basis of a mutational study, we show that not only the presence of the phytyls phytyls is necessary for photoprotection in WSCPs, as we previously demonstrated, but also is their correct correct conformation and localization. The...
This data repository is not currently reporting usage information. For information on how your repository can submit usage information, please see our documentation.