Section 70
Chapter 69,285

Stability of Water-Soluble Chlorophyll Protein (WSCP) Depends on Phytyl Conformation

Palm, D.M.; Agostini, A.; Pohland, A.-C.; Werwie, M.; Jaenicke, E.; Paulsen, H.

Acs Omega 4(5): 7971-7979


ISSN/ISBN: 2470-1343
PMID: 31459885
DOI: 10.1021/acsomega.9b00054
Accession: 069284590

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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 pigments, the complex-bound Chls displays a remarkable stability toward photodynamic damage. On the basis of a mutational study, we show that not only the presence of the phytyls is necessary for photoprotection in WSCPs, as we previously demonstrated, but also is their correct conformation and localization. The extreme heat stability of WSCP also depends on the presence of the phytyl chains, confirming their relevance for the unusual stability of WSCP.

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