ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural rearrangements preceding dioxygen formation by the water oxidation complex of photosystem II.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 77 citations in OpenAlex.
- New Water Oxidation Mechanism in Photosystem II Resolves Major Experimental Controversies.Angewandte Chemie (International ed. in English) · 2026Article
- Structure of the D1-Val185Asn mutated photosystem II complex with slow O-O bond formation reveals changes in the Cl1 water channel.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Three rate-determining protein roles in photosynthetic ONature communications · 2025Article
- The Low Oxidation State Paradigm is More Consistent with XFEL Observations of the S₃ → [S₄] → S₀ Transition in Photosystem II.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Photosystem II: Probing Protons and Breaking Barriers.Biochemistry · 2025Review
- Mechanism of proton release during water oxidation in Photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Effect of Removal of External Proteins PsbO, PsbP and PsbQ on Flash-Induced Molecular Oxygen Evolution and Its Biphasicity in Tobacco PSII.Current issues in molecular biology · 2024Article
- Structure Function Studies of Photosystem II Using X-Ray Free Electron Lasers.Annual review of biophysics · 2024Review
- Review
- Bioinspired Active Site with a Coordination-Adaptive Organosulfonate Ligand for Catalytic Water Oxidation at Neutral pH.Journal of the American Chemical Society · 2023Article
- Structural evidence for intermediates during ONature · 2023Article
- Article
- Reversible Structural Isomerization of Nature's Water Oxidation Catalyst Prior to O-O Bond Formation.Journal of the American Chemical Society · 2022Article
- The exchange of the fast substrate water in the SChemical science · 2021Article
- Water oxidation in photosystem II.Photosynthesis research · 2019Review
- Energetics and Kinetics of S-State Transitions Monitored by Delayed Chlorophyll Fluorescence.Frontiers in plant science · 2019Article
- Gordon Research Conference on photosynthesis: photosynthetic plasticity from the environment to synthetic systems.Photosynthesis research · 2018Article
- ONature communications · 2018Article
- D1-Asn-298 in photosystem II is involved in a hydrogen-bond network near the redox-active tyrosine YThe Journal of biological chemistry · 2017Article
- Interaction of methanol with the oxygen-evolving complex: atomistic models, channel identification, species dependence, and mechanistic implications.Chemical science · 2016Article
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosynthetic water oxidation is catalyzed by the Mn4CaO5 cluster of photosystem II. Recent studies implicate an oxo bridge atom, O5, of the Mn4CaO5 cluster, as the "slowly exchanging" substrate water molecule. The D1-V185N mutant is in close vicinity of O5 and known to extend the lag phase and retard the O2 release phase (slow phase) in this critical last [Formula: see text] transition of water oxidation. The pH dependence, hydrogen/deuterium (H/D) isotope effect, and temperature dependence on the O2 release kinetics for this mutant were studied using time-resolved O2 polarography, and comparisons were made with WT and two mutants of the putative proton gate D1-D61. Both kinetic phases in V185N are independent of pH and buffer concentration and have weaker H/D kinetic isotope effects. Each phase is characterized by a parallel or even lower activation enthalpy but a less favorable activation entropy than the WT. The results indicate new rate-determining steps for both phases. It is concluded that the lag does not represent inhibition of proton release but rather, slowing of a previously unrecognized kinetic phase involving a structural rearrangement or tautomerism of the S3 (+) ground state as it approaches a configuration conducive to dioxygen formation. The parallel impacts on both the lag and O2 formation phases suggest a common origin for the defects surmised to be perturbations of the H-bond network and the water cluster adjacent to O5.
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