Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-122
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dc.contributor.authorPalm, Daniel
dc.contributor.authorAgostini, Alessandro
dc.contributor.authorPohland, Anne-Christin
dc.contributor.authorWerwie, Mara
dc.contributor.authorJaenicke, Elmar
dc.contributor.authorPaulsen, Harald
dc.date.accessioned2019-09-13T06:56:55Z
dc.date.available2019-09-13T08:56:55Z
dc.date.issued2019
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/124-
dc.description.abstractWater-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.en_GB
dc.description.sponsorshipDFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin
dc.language.isoeng
dc.rightsInCopyrightde_DE
dc.rights.urihttps://rightsstatements.org/vocab/InC/1.0/
dc.subject.ddc580 Pflanzen (Botanik)de_DE
dc.subject.ddc580 Botanical sciencesen_GB
dc.titleStability of water-soluble chlorophyll protein (WSCP) depends on phytyl conformationen_GB
dc.typeZeitschriftenaufsatzde_DE
dc.identifier.urnurn:nbn:de:hebis:77-publ-592353
dc.identifier.doihttp://doi.org/10.25358/openscience-122-
jgu.type.dinitypearticle
jgu.type.versionPublished versionen_GB
jgu.type.resourceText
jgu.organisation.departmentFB 10 Biologie-
jgu.organisation.departmentFB 09 Chemie, Pharmazie u. Geowissensch.-
jgu.organisation.number7950-
jgu.organisation.number7970-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleACS omega
jgu.journal.volume4
jgu.journal.issue5
jgu.pages.start7971
jgu.pages.end7979
jgu.publisher.year2019
jgu.publisher.nameACS Publications
jgu.publisher.placeWashington, DC
jgu.publisher.urihttp://dx.doi.org/10.1021/acsomega.9b00054
jgu.publisher.issn2470-1343
jgu.organisation.placeMainz-
jgu.subject.ddccode580
opus.date.accessioned2019-09-13T06:56:55Z
opus.date.modified2019-09-13T07:02:16Z
opus.date.available2019-09-13T08:56:55
opus.subject.dfgcode00-000
opus.organisation.stringFB 10: Biologie: Institut für Molekulare Physiologiede_DE
opus.organisation.stringFB 09: Chemie, Pharmazie und Geowissenschaften: Institut für Pharmazie und Biochemiede_DE
opus.identifier.opusid59235
opus.institute.number1013
opus.institute.number0910
opus.metadataonlyfalse
opus.type.contenttypeKeinede_DE
opus.type.contenttypeNoneen_GB
opus.affiliatedPalm, Daniel
opus.affiliatedPohland, Anne-Christin
opus.affiliatedWerwie, Mara
opus.affiliatedJaenicke, Elmar
opus.affiliatedPaulsen, Harald
jgu.publisher.doi10.1021/acsomega.9b00054
jgu.organisation.rorhttps://ror.org/023b0x485
Appears in collections:JGU-Publikationen

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