Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-122
Authors: Palm, Daniel
Agostini, Alessandro
Pohland, Anne-Christin
Werwie, Mara
Jaenicke, Elmar
Paulsen, Harald
Title: Stability of water-soluble chlorophyll protein (WSCP) depends on phytyl conformation
Online publication date: 13-Sep-2019
Language: english
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 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 extreme heat stability of WSCP also depends on the presence presence of the phytyl chains, confirming their relevance for the unusual stability of WSCP.
DDC: 580 Pflanzen (Botanik)
580 Botanical sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 10 Biologie
FB 09 Chemie, Pharmazie u. Geowissensch.
Place: Mainz
DOI: http://doi.org/10.25358/openscience-122
URN: urn:nbn:de:hebis:77-publ-592353
Version: Published version
Publication type: Zeitschriftenaufsatz
License: in Copyright
Information on rights of use: https://rightsstatements.org/vocab/InC/1.0/
Journal: ACS omega
4
5
Pages or article number: 7971
7979
Publisher: ACS Publications
Publisher place: Washington, DC
Issue date: 2019
ISSN: 2470-1343
Publisher URL: http://dx.doi.org/10.1021/acsomega.9b00054
Publisher DOI: 10.1021/acsomega.9b00054
Appears in collections:JGU-Publikationen

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