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

ABSTRACT: 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.

SUBMITTER: Palm DM

PROVIDER: S-EPMC6648419 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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

Palm Daniel M DM Agostini Alessandro A Pohland Anne-Christin AC Werwie Mara M Jaenicke Elmar E Paulsen Harald H

ACS omega 20190501 5

Water-soluble chlorophyll proteins (WSCP) from <i>Brassicaceae</i> 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 conformatio ...[more]

PMID: 31459885

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