ReviewAnnual review of biophysics2024
Structure Function Studies of Photosystem II Using X-Ray Free Electron Lasers.
Review in Annual review of biophysics, 2024. 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.
- High-Valent Late Transition Metal-Oxo Complexes: Breaking Boundaries at the Oxo Wall and Beyond.Chemical reviews · 2026Review
- Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase.Nature communications · 2026Article
- Photosystem II: commonality and diversity with emphasis on the extrinsic subunits.Plant & cell physiology · 2025Review
- Current perspectives on proton and electron transfer pathways in photosystem II water oxidation.Plant & cell physiology · 2025Review
- 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
- Photosystem II: Probing Protons and Breaking Barriers.Biochemistry · 2025Review
- X-ray Absorption Spectroscopy of Dilute Metalloenzymes at X-ray Free-Electron Lasers in a Shot-by-Shot Mode.The journal of physical chemistry letters · 2025Article
- High-Spin Manganese(V) in an Active Center Analogue of the Oxygen-Evolving Complex.Journal of the American Chemical Society · 2025Article
- Exploring the Structural Diversity and Evolution of the D1 Subunit of Photosystem II Using AlphaFold and Foldtree.Physiologia plantarumArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The structure and mechanism of the water-oxidation chemistry that occurs in photosystem II have been subjects of great interest. The advent of X-ray free electron lasers allowed the determination of structures of the stable intermediate states and of steps in the transitions between these intermediate states, bringing a new perspective to this field. The room-temperature structures collected as the photosynthetic water oxidation reaction proceeds in real time have provided important novel insights into the structural changes and the mechanism of the water oxidation reaction. The time-resolved measurements have also given us a view of how this reaction-which involves multielectron, multiproton processes-is facilitated by the interaction of the ligands and the protein residues in the oxygen-evolving complex. These structures have also provided a picture of the dynamics occurring in the channels within photosystem II that are involved in the transport of the substrate water to the catalytic center and protons to the bulk.
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What OpenQuestion holds
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.