Carotenoid-induced non-photochemical quenching in the cyanobacterial chlorophyll synthase-HliC/D complex

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388971:_____/16:00467874

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Carotenoid-induced non-photochemical quenching in the cyanobacterial chlorophyll synthase-HliC/D complex

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Carotenoid-induced non-photochemical quenching in the cyanobacterial chlorophyll synthase-HliC/D complex

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

<a href="/cs/project/GBP501%2F12%2FG055" target="_blank" >GBP501/12/G055: Centrum fotosyntetického výzkumu</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biochimica et Biophysica Acta - Bioenergetics

ISSN

0005-2728

e-ISSN

—

Svazek periodika

1857

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

1430-1439

Kód UT WoS článku

000382590400009

EID výsledku v databázi Scopus

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