Structural dynamics in the water and proton channels of photosystem II during the S2 to S3 transition


Details zur Publikation

Autor*innen: Hussein R., Ibrahim M., Bhowmick A., Simon P.S., Chatterjee R., Lassalle L., Doyle M., Bogacz I., Kim I.S., Cheah M.H., Gul S., de Lichtenberg C., Chernev P., Pham C.C., Young I.D., Carbajo S., Fuller F.D., Alonso-Mori R., Batyuk A., Sutherlin K.D., Brewster A.S., Bolotovsky R., Mendez D., Holton J.M., Moriarty N.W., Adams P.D., Bergmann U., Sauter N.K., Dobbek H., Messinger J., Zouni A., Kern J., Yachandra V.K., Yano J.

Zeitschrift: Nature Communications

Jahr der Veröffentlichung: 2021

Bandnummer: 12

Heftnummer: 1

Verlag: Nature Publishing Group: Nature Communications

ISSN: 2041-1723

eISSN: 2041-1723

DOI: 10.1038/s41467-021-26781-z


Sprachen: English-Great Britain


Light-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.


Zuletzt aktualisiert 2022-28-09 um 19:47