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