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

Result code in 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>

Alternative codes found

RIV/61388971:_____/20:00524372

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/GA15-12816S" target="_blank" >GA15-12816S: Theoretical Study of Photosyntetic Processes in Photosystem II</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

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

Name of the periodical

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

—

Volume of the periodical

26

Issue of the periodical within the volume

4

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

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UT code for WoS article

000519593600001

EID of the result in the Scopus database

2-s2.0-85081563370