Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00604426" target="_blank" >RIV/60077344:_____/24:00604426 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/24:43908355

Výsledek na webu

<a href="https://www.science.org/doi/10.1126/sciadv.adk7535" target="_blank" >https://www.science.org/doi/10.1126/sciadv.adk7535</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1126/sciadv.adk7535" target="_blank" >10.1126/sciadv.adk7535</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes

Popis výsledku v původním jazyce

Cyanobacteria use large antenna complexes called phycobilisomes (PBSs) for light harvesting. However, intense light triggers non-photochemical quenching, where the orange carotenoid protein (OCP) binds to PBS, dissipating excess energy as heat. The mechanism of efficiently transferring energy from phycocyanobilins in PBS to canthaxanthin in OCP remains insufficiently understood. Using cryo-electron microscopy, we unveiled the OCP-PBS complex structure at 1.6- to 2.1-angstrom resolution, showcasing its inherent flexibility. Using multiscale quantum chemistry, we disclosed the quenching mechanism. Identifying key protein residues, we clarified how canthaxanthin's transition dipole moment in its lowest-energy dark state becomes large enough for efficient energy transfer from phycocyanobilins. Our energy transfer model offers a detailed understanding of the atomic determinants of light harvesting regulation and antenna architecture in cyanobacteria.

Název v anglickém jazyce

Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes

Popis výsledku anglicky

Cyanobacteria use large antenna complexes called phycobilisomes (PBSs) for light harvesting. However, intense light triggers non-photochemical quenching, where the orange carotenoid protein (OCP) binds to PBS, dissipating excess energy as heat. The mechanism of efficiently transferring energy from phycocyanobilins in PBS to canthaxanthin in OCP remains insufficiently understood. Using cryo-electron microscopy, we unveiled the OCP-PBS complex structure at 1.6- to 2.1-angstrom resolution, showcasing its inherent flexibility. Using multiscale quantum chemistry, we disclosed the quenching mechanism. Identifying key protein residues, we clarified how canthaxanthin's transition dipole moment in its lowest-energy dark state becomes large enough for efficient energy transfer from phycocyanobilins. Our energy transfer model offers a detailed understanding of the atomic determinants of light harvesting regulation and antenna architecture in cyanobacteria.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

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

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

Science Advances

ISSN

2375-2548

e-ISSN

2375-2548

Svazek periodika

10

Číslo periodika v rámci svazku

14

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

eadk7535

Kód UT WoS článku

001198102900002

EID výsledku v databázi Scopus

2-s2.0-85190085264