Photoprotection of photosynthetic pigments in plant one-helix protein 1/2 heterodimers.
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Photoprotection of photosynthetic pigments in plant one-helix protein 1/2 heterodimers.
Original language description
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.
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
10610 - Biophysics
Result continuities
Project
<a href="/en/project/GA20-01159S" target="_blank" >GA20-01159S: Interactions between pigments for efficient light harvesting and photoprotection in photosynthesis</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
Journal of Physical Chemistry Letters
ISSN
1948-7185
e-ISSN
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Volume of the periodical
11
Issue of the periodical within the volume
21
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
9387-9392
UT code for WoS article
000589920000066
EID of the result in the Scopus database
2-s2.0-85095799967