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Violaxanthin and Zeaxanthin May Replace Lutein at the L1 Site of LHCII, Conserving the Interactions with Surrounding Chlorophylls and the Capability of Triplet-Triplet Energy Transfer

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F22%3A00568346" target="_blank" >RIV/60077344:_____/22:00568346 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.mdpi.com/1422-0067/23/9/4812" target="_blank" >https://www.mdpi.com/1422-0067/23/9/4812</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms23094812" target="_blank" >10.3390/ijms23094812</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Violaxanthin and Zeaxanthin May Replace Lutein at the L1 Site of LHCII, Conserving the Interactions with Surrounding Chlorophylls and the Capability of Triplet-Triplet Energy Transfer

  • Original language description

    Carotenoids represent the first line of defence of photosystems against singlet oxygen (O-1(2)) toxicity, because of their capacity to quench the chlorophyll triplet state ((3)Chl) through a physical mechanism based on the transfer of triplet excitation (triplet-triplet energy transfer, TTET). In previous works, we showed that the antenna LHCII is characterised by a robust photoprotective mechanism, able to adapt to the removal of individual chlorophylls while maintaining a remarkable capacity for (3)Chl quenching. In this work, we investigated the effects on this quenching induced in LHCII by the replacement of the lutein bound at the L1 site with violaxanthin and zeaxanthin. We studied LHCII isolated from the Arabidopsis thaliana mutants lut2-in which lutein is replaced by violaxanthin-and lut2 npq2, in which all xanthophylls are replaced constitutively by zeaxanthin. We characterised the photophysics of these systems via optically detected magnetic resonance (ODMR) and time-resolved electron paramagnetic resonance (TR-EPR). We concluded that, in LHCII, lutein-binding sites have conserved characteristics, and ensure efficient TTET regardless of the identity of the carotenoid accommodated.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

    <a href="/en/project/EF18_053%2F0016982" target="_blank" >EF18_053/0016982: International mobilities for researchers and administrative employees of Biology Centre</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    International Journal of Molecular Sciences

  • ISSN

    1422-0067

  • e-ISSN

    1422-0067

  • Volume of the periodical

    23

  • Issue of the periodical within the volume

    9

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    13

  • Pages from-to

    4812

  • UT code for WoS article

    000794440100001

  • EID of the result in the Scopus database

    2-s2.0-85128734080