Carotenoid-induced non-photochemical quenching in the cyanobacterial chlorophyll synthase-HliC/D complex
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F16%3A43890796" target="_blank" >RIV/60076658:12310/16:43890796 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/16:00467874
Result on the web
<a href="http://www.sciencedirect.com/science/article/pii/S0005272816303796" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0005272816303796</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbabio.2016.04.280" target="_blank" >10.1016/j.bbabio.2016.04.280</a>
Alternative languages
Result language
angličtina
Original language name
Carotenoid-induced non-photochemical quenching in the cyanobacterial chlorophyll synthase-HliC/D complex
Original language description
Chl synthase (ChlG) is an important enzyme of the Chl biosynthetic pathway catalyzing attachment of phytol/geranylgeraniol tail to the chlorophyllide molecule. Here we have investigated the Flag-tagged ChlG (f.ChlG) in a complex with two different high-light inducible proteins (Hlips) HliD and HliC. The f.ChlG-Hlips complex binds a Chl alpha and three different carotenoids, beta-carotene, zeaxanthin and myxoxanthophyll. Application of ultra fast time-resolved absorption spectroscopy performed at room and cryogenic temperatures revealed excited state dynamics of complex-bound pigments. After excitation of Chl alpha in the complex, excited Chl a is efficiently quenched by a nearby carotenoid molecule via energy transfer from the Chl alpha Q(y) state to the carotenoid S-1 state. The kinetic analysis of the spectroscopic data revealed that quenching occurs with a time constant of similar to 2 ps and its efficiency is temperature independent. Even though due to its long conjugation myxoxanthophyll appears to be energetically best suited for role of Chl alpha quencher, based on comparative analysis and spectroscopic data we propose that beta-carotene bound to Hlips acts as the quencher rather than myxoxanthophyll and zeaxanthin, which are bound at the f.ChlG and Hlips interface. The S-1 state lifetime of the quencher has been determined to be 13 ps at room temperature and 21 ps at 77 K. These results demonstrate that Hlips act as a conserved functional module that prevents photodamage of protein complexes during photosystem assembly or Chl biosynthesis.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GBP501%2F12%2FG055" target="_blank" >GBP501/12/G055: Photosynthesis Research Center</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochimica et Biophysica Acta - Bioenergetics
ISSN
0005-2728
e-ISSN
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Volume of the periodical
1857
Issue of the periodical within the volume
9
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
10
Pages from-to
1430-1439
UT code for WoS article
000382590400009
EID of the result in the Scopus database
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