ReviewBiochemistry2025
Photosystem II: Probing Protons and Breaking Barriers.
Review in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- 24-Epibrassinolide enhances aluminum tolerance in tobacco through Ca²⁺-dependent signaling, antioxidant regulation, and metal homeostasis.Plant signaling & behavior · 2026Article
- New Water Oxidation Mechanism in Photosystem II Resolves Major Experimental Controversies.Angewandte Chemie (International ed. in English) · 2026Article
- Molecular basis for alternative charge separation pathways in type-II photosynthetic reaction centers.PNAS nexus · 2026Article
- Living Photoanodes for Solar-Driven Water Oxidation.Chemical reviews · 2026Review
- Current perspectives on proton and electron transfer pathways in photosystem II water oxidation.Plant & cell physiology · 2025Review
- Photosystem II: commonality and diversity with emphasis on the extrinsic subunits.Plant & cell physiology · 2025Review
- Electronic Structure of the SACS physical chemistry Au · 2025Article
- Revisiting the Proposed Protonated Water Cluster at the Exit Site of the Proton Transfer Pathway in Bacteriorhodopsin.The journal of physical chemistry. B · 2025Article
- Energetics of tryptophan residues in electron transfer and photoprotection of type-II photosynthetic reaction centers.PNAS nexus · 2025Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosystem II (PSII) is a multisubunit protein-pigment complex that drives the oxidation of water, producing molecular oxygen essential for life. At the core of PSII, the oxygen-evolving complex (OEC) facilitates sequential four-electron oxidation steps following the Kok cycle. Despite significant progress in structural and spectroscopic studies, fundamental questions remain regarding the precise mechanisms of substrate water incorporation, deprotonation pathways, and oxygen-oxygen bond formation. A key challenge is determining the protonation states of water ligands and oxo bridges in the OEC, as incorrect assignments can eventually lead to misinterpretation of reaction energetics and mechanisms. This Review examines recent structural, spectroscopic, and theoretical studies, with a particular focus on proton transfer pathways and the role of key residues in regulating OEC deprotonation, emphasizing the importance of systematically establishing protonation states at lower S-states before modeling higher oxidation states. By integrating structural data with fundamental chemical principles, we outline essential considerations for constructing a physically meaningful and mechanistically coherent model of water oxidation in PSII.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.