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Title | Cryo-electron microscopy reveals hydrogen positions and water networks in photosystem II. |
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Journal, issue, pages | Science, Vol. 384, Issue 6702, Page 1349-1355, Year 2024 |
Publish date | Jun 21, 2024 |
Authors | Rana Hussein / André Graça / Jack Forsman / A Orkun Aydin / Michael Hall / Julia Gaetcke / Petko Chernev / Petra Wendler / Holger Dobbek / Johannes Messinger / Athina Zouni / Wolfgang P Schröder / |
PubMed 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 ...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 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. |
External links | Science / PubMed:38900892 |
Methods | EM (single particle) |
Resolution | 1.71 Å |
Structure data | EMDB-50019, PDB-9evx: |
Chemicals | ChemComp-FE2: ChemComp-CL: ChemComp-CLA: ChemComp-BCR: ChemComp-PL9: ChemComp-STE: ChemComp-LMG: ChemComp-SQD: ChemComp-DGD: ChemComp-OEX: ChemComp-PHO: ChemComp-LHG: ChemComp-LMT: ChemComp-BCT: ChemComp-HEM: ChemComp-HEC: ChemComp-HOH: |
Source |
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Keywords | METAL BINDING PROTEIN / Photosystem II core complex / Mn cluster / water oxidation |