Structural dynamics in the water and proton channels of photosystem II during the S2 to S3 transition
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Published:2021-11-11
Issue:1
Volume:12
Page:
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ISSN:2041-1723
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Container-title:Nature Communications
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language:en
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Short-container-title:Nat Commun
Author:
Hussein Rana, Ibrahim Mohamed, Bhowmick Asmit, Simon Philipp S.ORCID, Chatterjee Ruchira, Lassalle Louise, Doyle Margaret, Bogacz Isabel, Kim In-Sik, Cheah Mun Hon, Gul Sheraz, de Lichtenberg Casper, Chernev Petko, Pham Cindy C., Young Iris D.ORCID, Carbajo Sergio, Fuller Franklin D.ORCID, Alonso-Mori RobertoORCID, Batyuk Alex, Sutherlin Kyle D., Brewster Aaron S.ORCID, Bolotovsky Robert, Mendez Derek, Holton James M.ORCID, Moriarty Nigel W.ORCID, Adams Paul D.ORCID, Bergmann UweORCID, Sauter Nicholas K.ORCID, Dobbek HolgerORCID, Messinger JohannesORCID, Zouni AthinaORCID, Kern JanORCID, Yachandra Vittal K.ORCID, Yano JunkoORCID
Abstract
AbstractLight-driven oxidation of water to molecular oxygen is catalyzed by the oxygen-evolving complex (OEC) in Photosystem II (PS II). This multi-electron, multi-proton catalysis requires the transport of two water molecules to and four protons from the OEC. A high-resolution 1.89 Å structure obtained by averaging all the S states and refining the data of various time points during the S2 to S3 transition has provided better visualization of the potential pathways for substrate water insertion and proton release. Our results indicate that the O1 channel is the likely water intake pathway, and the Cl1 channel is the likely proton release pathway based on the structural rearrangements of water molecules and amino acid side chains along these channels. In particular in the Cl1 channel, we suggest that residue D1-E65 serves as a gate for proton transport by minimizing the back reaction. The results show that the water oxidation reaction at the OEC is well coordinated with the amino acid side chains and the H-bonding network over the entire length of the channels, which is essential in shuttling substrate waters and protons.
Funder
Caroline von Humboldt Stipendium, Humboldt University Berlin U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences DOE | Office of Science Deutsche Forschungsgemeinschaft Vetenskapsrådet DOE | SC | Chemical Sciences, Geosciences, and Biosciences Division
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Reference91 articles.
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