Journal
NATURE COMMUNICATIONS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms9488
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Funding
- JST PRESTO programme
- JSPS KAKENHI [22740276, 26800224, 15H00864, 25107517, 26105012, 26711008]
- Tokyo Ohka Foundation for Promotion of Science and Technology
- Biotechnological and Biological Sciences Research Council Grant [BB/K002627/1]
- Wolfson Merit Award of Royal Society
- Grants-in-Aid for Scientific Research [26711008, 25107517, 15H00864, 26105012, 26800224] Funding Source: KAKEN
- BBSRC [BB/K002627/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K002627/1] Funding Source: researchfish
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In photosystem II (PSII), the Mn4CaO5 cluster catalyses the water splitting reaction. The crystal structure of PSII shows the presence of a hydrogen-bonded water molecule directly linked to O4. Here we show the detailed properties of the H-bonds associated with the Mn4CaO5 cluster using a quantum mechanical/molecular mechanical approach. When O4 is taken as a mu-hydroxo bridge acting as a hydrogen-bond donor to water539 (W539), the S-0 redox state best describes the unusually short O4-OW539 distance (2.5 angstrom) seen in the crystal structure. We find that in S-1, O4 easily releases the proton into a chain of eight strongly hydrogen-bonded water molecules. The corresponding hydrogen-bond network is absent for O5 in S-1. The present study suggests that the O4-water chain could facilitate the initial deprotonation event in PSII. This unexpected insight is likely to be of real relevance to mechanistic models for water oxidation.
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