Triplet state quenching of bacteriochlorophyll c aggregates in a protein-free environment of a chlorosome interior
The result's identifiers
Result code in 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>
Alternative codes found
RIV/60077344:_____/20:00517107 RIV/61388955:_____/20:00517107 RIV/00216208:11320/20:10404684
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Triplet state quenching of bacteriochlorophyll c aggregates in a protein-free environment of a chlorosome interior
Original language description
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.
Czech name
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Czech description
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Classification
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
10403 - Physical chemistry
Result continuities
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)
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Chemical Physics
ISSN
0301-0104
e-ISSN
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Volume of the periodical
529
Issue of the periodical within the volume
JAN 15 2020
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
7
Pages from-to
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UT code for WoS article
000498052700002
EID of the result in the Scopus database
2-s2.0-85072961984