The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901340" target="_blank" >RIV/60076658:12310/20:43901340 - isvavai.cz</a>
Result on the web
<a href="https://pubs.rsc.org/en/content/articlelanding/2020/PP/D0PP00174K#!divAbstract" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2020/PP/D0PP00174K#!divAbstract</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/d0pp00174k" target="_blank" >10.1039/d0pp00174k</a>

Result language
angličtina
Original language name
The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection
Original language description
Xanthophylls in light harvesting complexes perform a number of functions ranging from structural support to light-harvesting and photoprotection. In the major light harvesting complex of photosystem II in plants (LHCII), the innermost xanthophyll binding pockets are occupied by lutein molecules. The conservation of these sites within the LHC protein family suggests their importance in LHCII functionality. In the present work, we induced the photoprotective switch in LHCII isolated from theArabidopsismutantnpq1lut2, where the lutein molecules are exchanged with violaxanthin. Despite the differences in the energetics of the pigments and the impairment of chlorophyll fluorescence quenchingin vivo, we show that isolated complexes containing violaxanthin are still able to induce the quenching switch to a similar extent to wild type LHCII monomers. Moreover, the same spectroscopic changes take place, which suggest the involvement of the terminal emitter site (L1) in energy dissipation in both complexes. These results indicate the robust nature of the L1 xanthophyll binding domain in LHCII, where protein structural cues are the major determinant of the function of the bound carotenoid.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics

Project
<a href="/en/project/GX19-28323X" target="_blank" >GX19-28323X: Relation between structure and function of carotenoids: New pathways to answer unresolved questions</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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