ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure of Sr-substituted photosystem II at 2.1 A resolution and its implications in the mechanism of water oxidation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed.
- Asymmetric Connectivity Between Redox-Active Tyrosines and Reaction-Center Chlorophylls in Photosystem II.Plants (Basel, Switzerland) · 2026Article
- PEO-sheathed liquid jets increase sample delivery stability for serial femtosecond X-ray crystallography.Scientific reports · 2026Article
- An analysis of the structural changes of the oxygen evolving complex of Photosystem II in the SBiochimica et biophysica acta. Bioenergetics · 2025Review
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- Excitation landscape of the CP43 photosynthetic antenna complex from multiscale simulations.Chemical science · 2024Article
- Interplay of two low-barrier hydrogen bonds in long-distance proton-coupled electron transfer for water oxidation.PNAS nexus · 2023Article
- Structural and energetic insights into Mn-to-Fe substitution in the oxygen-evolving complex.iScience · 2023Article
- Article
- Predicting the oxidation states of Mn ions in the oxygen-evolving complex of photosystem II using supervised and unsupervised machine learning.Photosynthesis research · 2023Article
- Heterologous expression, purification and structural features of nativeFrontiers in chemistry · 2023Article
- Functional Water Networks in Fully Hydrated Photosystem II.Journal of the American Chemical Society · 2022Article
- Macromolecular conformational changes in photosystem II: interaction between structure and function.Biophysical reviews · 2022Review
- Co-flow injection for serial crystallography at X-ray free-electron lasers.Journal of applied crystallography · 2022Article
- Mimicking the Oxygen-Evolving Center in Photosynthesis.Frontiers in plant science · 2022Review
- Role of redox-inactive metals in controlling the redox potential of heterometallic manganese-oxido clusters.Photosynthesis research · 2021Article
- High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams.Communications biology · 2021Article
- Structural basis of light-harvesting in the photosystem II core complex.Protein science : a publication of the Protein Society · 2020Review
- The study of conformational changes in photosystem II during a charge separation.Journal of molecular modeling · 2020Article
- Redox Tuning via Ligand-Induced Geometric Distortions at a YMnInorganic chemistry · 2019Article
- Water oxidation in photosystem II.Photosynthesis research · 2019Review
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Abstract
Oxygen-evolving complex of photosystem II (PSII) is a tetra-manganese calcium penta-oxygenic cluster (Mn4CaO5) catalyzing light-induced water oxidation through several intermediate states (S-states) by a mechanism that is not fully understood. To elucidate the roles of Ca(2+) in this cluster and the possible location of water substrates in this process, we crystallized Sr(2+)-substituted PSII from Thermosynechococcus vulcanus, analyzed its crystal structure at a resolution of 2.1 Å, and compared it with the 1.9 Å structure of native PSII. Our analysis showed that the position of Sr was moved toward the outside of the cubane structure of the Mn4CaO5-cluster relative to that of Ca(2+), resulting in a general elongation of the bond distances between Sr and its surrounding atoms compared with the corresponding distances in the Ca-containing cluster. In particular, we identified an apparent elongation in the bond distance between Sr and one of the two terminal water ligands of Ca(2+), W3, whereas that of the Sr-W4 distance was not much changed. This result may contribute to the decrease of oxygen evolution upon Sr(2+)-substitution, and suggests a weak binding and rather mobile nature of this particular water molecule (W3), which in turn implies the possible involvement of this water molecule as a substrate in the O-O bond formation. In addition, the PsbY subunit, which was absent in the 1.9 Å structure of native PSII, was found in the Sr-PSII structure.
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