Cryo–electron microscopy reveals hydrogen positions and water networks in photosystem II. Hussein, R., Graça, A., Forsman, J., Aydin, A. O., Hall, M., Gaetcke, J., Chernev, P., Wendler, P., Dobbek, H., Messinger, J., Zouni, A., & Schröder, W. P. Science, 384(6702):1349–1355, June, 2024. Publisher: American Association for the Advancement of Science![Cryo–electron microscopy reveals hydrogen positions and water networks in photosystem II [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Photosystem II starts the photosynthetic electron transport chain that converts solar energy into chemical energy and thus sustains life on Earth. It catalyzes two chemical reactions: water oxidation to molecular oxygen and plastoquinone reduction. Coupling of electron and proton transfer is crucial for efficiency; however, the molecular basis of these processes remains speculative owing to uncertain water binding sites and the lack of experimentally determined hydrogen positions. We thus collected high-resolution cryo–electron microscopy data of fully hydrated photosystem II from the thermophilic cyanobacterium Thermosynechococcus vestitus to a final resolution of 1.71 angstroms. The structure reveals several previously undetected partially occupied water binding sites and more than half of the hydrogen and proton positions. This clarifies the pathways of substrate water binding and plastoquinone B protonation.
@article{hussein_cryoelectron_2024,
title = {Cryo–electron microscopy reveals hydrogen positions and water networks in photosystem {II}},
volume = {384},
url = {https://www.science.org/doi/10.1126/science.adn6541},
doi = {10.1126/science.adn6541},
abstract = {Photosystem II starts the photosynthetic electron transport chain that converts solar energy into chemical energy and thus sustains life on Earth. It catalyzes two chemical reactions: water oxidation to molecular oxygen and plastoquinone reduction. Coupling of electron and proton transfer is crucial for efficiency; however, the molecular basis of these processes remains speculative owing to uncertain water binding sites and the lack of experimentally determined hydrogen positions. We thus collected high-resolution cryo–electron microscopy data of fully hydrated photosystem II from the thermophilic cyanobacterium Thermosynechococcus vestitus to a final resolution of 1.71 angstroms. The structure reveals several previously undetected partially occupied water binding sites and more than half of the hydrogen and proton positions. This clarifies the pathways of substrate water binding and plastoquinone B protonation.},
number = {6702},
urldate = {2024-06-26},
journal = {Science},
author = {Hussein, Rana and Graça, André and Forsman, Jack and Aydin, A. Orkun and Hall, Michael and Gaetcke, Julia and Chernev, Petko and Wendler, Petra and Dobbek, Holger and Messinger, Johannes and Zouni, Athina and Schröder, Wolfgang P.},
month = jun,
year = {2024},
note = {Publisher: American Association for the Advancement of Science},
pages = {1349--1355},
}
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Coupling of electron and proton transfer is crucial for efficiency; however, the molecular basis of these processes remains speculative owing to uncertain water binding sites and the lack of experimentally determined hydrogen positions. We thus collected high-resolution cryo–electron microscopy data of fully hydrated photosystem II from the thermophilic cyanobacterium Thermosynechococcus vestitus to a final resolution of 1.71 angstroms. The structure reveals several previously undetected partially occupied water binding sites and more than half of the hydrogen and proton positions. 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It catalyzes two chemical reactions: water oxidation to molecular oxygen and plastoquinone reduction. Coupling of electron and proton transfer is crucial for efficiency; however, the molecular basis of these processes remains speculative owing to uncertain water binding sites and the lack of experimentally determined hydrogen positions. We thus collected high-resolution cryo–electron microscopy data of fully hydrated photosystem II from the thermophilic cyanobacterium Thermosynechococcus vestitus to a final resolution of 1.71 angstroms. The structure reveals several previously undetected partially occupied water binding sites and more than half of the hydrogen and proton positions. This clarifies the pathways of substrate water binding and plastoquinone B protonation.},\n\tnumber = {6702},\n\turldate = {2024-06-26},\n\tjournal = {Science},\n\tauthor = {Hussein, Rana and Graça, André and Forsman, Jack and Aydin, A. 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