The study of conformational changes in photosystem II during a charge separation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901221" target="_blank" >RIV/60076658:12310/20:43901221 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/20:00524372

Výsledek na webu

<a href="https://link.springer.com/article/10.1007%2Fs00894-020-4332-9" target="_blank" >https://link.springer.com/article/10.1007%2Fs00894-020-4332-9</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-020-4332-9" target="_blank" >10.1007/s00894-020-4332-9</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The study of conformational changes in photosystem II during a charge separation

Popis výsledku v původním jazyce

Photosystem II (PSII) is a multi-subunit pigment-protein complex and is one of several protein assemblies that function cooperatively in photosynthesis in plants and cyanobacteria. As more structural data on PSII become available, new questions arise concerning the nature of the charge separation in PSII reaction center (RC). The crystal structure of PSII RC from cyanobacteria Thermosynechococcus vulcanus was selected for the computational study of conformational changes in photosystem II associated to the charge separation process. The parameterization of cofactors and lipids for classical MD simulation with Amber force field was performed. The parametrized complex of PSII was embedded in the lipid membrane for MD simulation with Amber in Gromacs. The conformational behavior of protein and the cofactors directly involved in the charge separation were studied by MD simulations and QM/MM calculations. This study identified the most likely mechanism of the proton-coupled reduction of plastoquinone Q(B). After the charge separation and the first electron transfer to Q(B), the system undergoes conformational change allowing the first proton transfer to Q(B)(-) mediated via Ser264. After the second electron transfer to Q(B)H, the system again adopts conformation allowing the second proton transfer to Q(B)H(-). The reduced Q(B)H(2) would then leave the binding pocket.

Název v anglickém jazyce

The study of conformational changes in photosystem II during a charge separation

Popis výsledku anglicky

Photosystem II (PSII) is a multi-subunit pigment-protein complex and is one of several protein assemblies that function cooperatively in photosynthesis in plants and cyanobacteria. As more structural data on PSII become available, new questions arise concerning the nature of the charge separation in PSII reaction center (RC). The crystal structure of PSII RC from cyanobacteria Thermosynechococcus vulcanus was selected for the computational study of conformational changes in photosystem II associated to the charge separation process. The parameterization of cofactors and lipids for classical MD simulation with Amber force field was performed. The parametrized complex of PSII was embedded in the lipid membrane for MD simulation with Amber in Gromacs. The conformational behavior of protein and the cofactors directly involved in the charge separation were studied by MD simulations and QM/MM calculations. This study identified the most likely mechanism of the proton-coupled reduction of plastoquinone Q(B). After the charge separation and the first electron transfer to Q(B), the system undergoes conformational change allowing the first proton transfer to Q(B)(-) mediated via Ser264. After the second electron transfer to Q(B)H, the system again adopts conformation allowing the second proton transfer to Q(B)H(-). The reduced Q(B)H(2) would then leave the binding pocket.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA15-12816S" target="_blank" >GA15-12816S: Teoretické studium fotosyntetických procesů ve fotosystému II</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

—

Svazek periodika

26

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

000519593600001

EID výsledku v databázi Scopus

2-s2.0-85081563370