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Triplet state quenching of bacteriochlorophyll c aggregates in a protein-free environment of a chlorosome interior

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901163" target="_blank" >RIV/60076658:12310/20:43901163 - isvavai.cz</a>

  • Nalezeny alternativní kódy

    RIV/60077344:_____/20:00517107 RIV/61388955:_____/20:00517107 RIV/00216208:11320/20:10404684

  • Výsledek na webu

    <a href="https://www.sciencedirect.com/science/article/pii/S0301010419305920?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0301010419305920?via%3Dihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.chemphys.2019.110542" target="_blank" >10.1016/j.chemphys.2019.110542</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Triplet state quenching of bacteriochlorophyll c aggregates in a protein-free environment of a chlorosome interior

  • Popis výsledku v původním jazyce

    Efficient quenching of (bacterio)chlorophyll triplet states by carotenoids prevents formation of reactive singlet oxygen in photosynthetic light-harvesting complexes. This protective process requires a close interaction between both types of pigments, which is usually ensured by a protein scaffold. Here we have studied quenching of bacteriochlorophyll c triplets in chlorosomes from the green photosynthetic bacterium Chloroflexus aurantiacus by nanosecond spectroscopy. Bacteriochlorophyll c forms aggregates in the chlorosome interior without involvement of a protein. We have observed that the triplet transfer from bacteriochlorophyll aggregates to carotenoids occurs with a transfer time of approximately 4 ns, being more than ten times slower that the estimates for the fastest triplet quenching in pigment-protein light-harvesting complexes. Nevertheless, together with aggregation-mediated shortening of excited state lifetimes, carotenoids provide efficient protection against formation of singlet oxygen in chlorosomes. Efficient triplet quenching was also observed in self-assembling, artificial light-harvesting complexes containing bacteriochlorophyll c aggregates and beta-carotene. This is important for their future applications in solar energy conversion. Finally, we have studied the temperature dependence of triplet quenching in chlorosomes and determined the activation energy of the energy transfer to be about 0.08 eV. This value lies within the range estimated for pigment-protein light-harvesting complexes.

  • Název v anglickém jazyce

    Triplet state quenching of bacteriochlorophyll c aggregates in a protein-free environment of a chlorosome interior

  • Popis výsledku anglicky

    Efficient quenching of (bacterio)chlorophyll triplet states by carotenoids prevents formation of reactive singlet oxygen in photosynthetic light-harvesting complexes. This protective process requires a close interaction between both types of pigments, which is usually ensured by a protein scaffold. Here we have studied quenching of bacteriochlorophyll c triplets in chlorosomes from the green photosynthetic bacterium Chloroflexus aurantiacus by nanosecond spectroscopy. Bacteriochlorophyll c forms aggregates in the chlorosome interior without involvement of a protein. We have observed that the triplet transfer from bacteriochlorophyll aggregates to carotenoids occurs with a transfer time of approximately 4 ns, being more than ten times slower that the estimates for the fastest triplet quenching in pigment-protein light-harvesting complexes. Nevertheless, together with aggregation-mediated shortening of excited state lifetimes, carotenoids provide efficient protection against formation of singlet oxygen in chlorosomes. Efficient triplet quenching was also observed in self-assembling, artificial light-harvesting complexes containing bacteriochlorophyll c aggregates and beta-carotene. This is important for their future applications in solar energy conversion. Finally, we have studied the temperature dependence of triplet quenching in chlorosomes and determined the activation energy of the energy transfer to be about 0.08 eV. This value lies within the range estimated for pigment-protein light-harvesting complexes.

Klasifikace

  • Druh

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

  • CEP obor

  • OECD FORD obor

    10403 - Physical chemistry

Návaznosti výsledku

  • Projekt

    <a href="/cs/project/GX19-28323X" target="_blank" >GX19-28323X: Vztah mezi strukturou a funkcí karotenoidů: Nové cesty k řešení nezodpovězených otázek</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

    Chemical Physics

  • ISSN

    0301-0104

  • e-ISSN

  • Svazek periodika

    529

  • Číslo periodika v rámci svazku

    JAN 15 2020

  • Stát vydavatele periodika

    NL - Nizozemsko

  • Počet stran výsledku

    7

  • Strana od-do

  • Kód UT WoS článku

    000498052700002

  • EID výsledku v databázi Scopus

    2-s2.0-85072961984