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Photoprotection of photosynthetic pigments in plant one-helix protein 1/2 heterodimers.

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F20%3A10421532" target="_blank" >RIV/00216208:11320/20:10421532 - isvavai.cz</a>

  • Výsledek na webu

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=qZ_0LVere_" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=qZ_0LVere_</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.jpclett.0c02660" target="_blank" >10.1021/acs.jpclett.0c02660</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Photoprotection of photosynthetic pigments in plant one-helix protein 1/2 heterodimers.

  • Popis výsledku v původním jazyce

    One-helix proteins 1 and 2 (OHP1/2) are members of the family of light-harvesting-like proteins (LIL) in plants, and their potential function(s) have been initially analyzed only recently. OHP1 and OHP2 are structurally related to the transmembrane α-helices 1 and 3 of all members of the light-harvesting complex (LHC) superfamily. Arabidopsis thaliana OHPs form heterodimers which bind 6 chlorophylls (Chls) a and two carotenoids in vitro. Their function remains unclear, and therefore, a spectroscopic study with reconstituted OHP1/OHP2-complexes was performed. Steady-state spectroscopy did not indicate singlet excitation energy transfer between pigments. Thus, a light-harvesting function can be excluded. Possible pigment-storage and/or -delivery functions of OHPs require photoprotection of the bound Chls. Hence, Chl and carotenoid triplet formation and decays in reconstituted OHP1/2 dimers were measured using nanosecond transient absorption spectroscopy. Unlike in all other photosynthetic LHCs, unquenched Chl triplets were observed with unusually long lifetimes. Moreover, there were virtually no differences in both Chl and carotenoid triplet state lifetimes under either aerobic or anaerobic conditions. The results indicate that both Chls and carotenoids are shielded by the proteins from interactions with ambient oxygen and, thus, protected against formation of singlet oxygen. Only a minor portion of the Chl triplets was quenched by carotenoids. These results are in stark contrast to all previously observed photoprotective processes in LHC/LIL proteins and, thus, may constitute a novel mechanism of photoprotection in the plant photosynthetic apparatus.

  • Název v anglickém jazyce

    Photoprotection of photosynthetic pigments in plant one-helix protein 1/2 heterodimers.

  • Popis výsledku anglicky

    One-helix proteins 1 and 2 (OHP1/2) are members of the family of light-harvesting-like proteins (LIL) in plants, and their potential function(s) have been initially analyzed only recently. OHP1 and OHP2 are structurally related to the transmembrane α-helices 1 and 3 of all members of the light-harvesting complex (LHC) superfamily. Arabidopsis thaliana OHPs form heterodimers which bind 6 chlorophylls (Chls) a and two carotenoids in vitro. Their function remains unclear, and therefore, a spectroscopic study with reconstituted OHP1/OHP2-complexes was performed. Steady-state spectroscopy did not indicate singlet excitation energy transfer between pigments. Thus, a light-harvesting function can be excluded. Possible pigment-storage and/or -delivery functions of OHPs require photoprotection of the bound Chls. Hence, Chl and carotenoid triplet formation and decays in reconstituted OHP1/2 dimers were measured using nanosecond transient absorption spectroscopy. Unlike in all other photosynthetic LHCs, unquenched Chl triplets were observed with unusually long lifetimes. Moreover, there were virtually no differences in both Chl and carotenoid triplet state lifetimes under either aerobic or anaerobic conditions. The results indicate that both Chls and carotenoids are shielded by the proteins from interactions with ambient oxygen and, thus, protected against formation of singlet oxygen. Only a minor portion of the Chl triplets was quenched by carotenoids. These results are in stark contrast to all previously observed photoprotective processes in LHC/LIL proteins and, thus, may constitute a novel mechanism of photoprotection in the plant photosynthetic apparatus.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10610 - Biophysics

Návaznosti výsledku

  • Projekt

    <a href="/cs/project/GA20-01159S" target="_blank" >GA20-01159S: Interakce mezi pigmenty pro účinný sběr světla a fotoprotekci ve fotosyntéze</a><br>

  • Návaznosti

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Ostatní

  • Rok uplatnění

    2020

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    Journal of Physical Chemistry Letters

  • ISSN

    1948-7185

  • e-ISSN

  • Svazek periodika

    11

  • Číslo periodika v rámci svazku

    21

  • Stát vydavatele periodika

    US - Spojené státy americké

  • Počet stran výsledku

    6

  • Strana od-do

    9387-9392

  • Kód UT WoS článku

    000589920000066

  • EID výsledku v databázi Scopus

    2-s2.0-85095799967