ReviewJournal of photochemistry and photobiology. B, Biology
Proton coupled electron transfer and redox active tyrosines in Photosystem II.
Review in Journal of photochemistry and photobiology. B, Biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 75 citations in OpenAlex.
- Modulating Radical Propagation in Proteins by Proton-Coupled Electron Transfer and Hydrogen Bonding.Biochemistry · 2026Article
- Asymmetric Connectivity Between Redox-Active Tyrosines and Reaction-Center Chlorophylls in Photosystem II.Plants (Basel, Switzerland) · 2026Article
- Interrelated Roles of Chloride and Bicarbonate in Regulating Electron Transport Across Photosystem II inPlants (Basel, Switzerland) · 2026Article
- Modulating radical propagation in proteins by proton-coupled electron transfer and hydrogen bonding.bioRxiv : the preprint server for biology · 2026Article
- Multisite Proton-Coupled Electron Transfer at a Keggin-Type Polyoxotungstate.Journal of the American Chemical Society · 2026Article
- Tyrosine residues initiated photopolymerization in living organisms.Nature communications · 2023Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Directed Electron Transfer in Flavin Peptides with Oligoproline-Type Helical Conformation as Models for Flavin-Functional Proteins.ChemistryOpen · 2020Article
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- Substituent Effects on Photochemistry of Anthracene-Phenol-Pyridine Triads Revealed by Multireference Calculations.Journal of the American Chemical Society · 2020Article
- Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping.Journal of the American Chemical Society · 2019Article
- Structure and Function of Tryptophan-Tyrosine Dyads in Biomimetic β Hairpins.The journal of physical chemistry. B · 2019Article
- Intramolecular Photogeneration of a Tyrosine Radical in a Designed Protein.ChemPhotoChem · 2017Article
- Critical Aspects of Heme-Peroxo-Cu Complex Structure and Nature of Proton Source Dictate Metal-O(peroxo) Breakage versus Reductive O-O Cleavage Chemistry.Journal of the American Chemical Society · 2017Article
- Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II.The journal of physical chemistry. B · 2016Article
- Stopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated Electron Transfer Pathway in Peptidylglycine Monooxygenase.Biochemistry · 2016Article
- Direct Interfacial YChemical science · 2015Article
- Influence of thylakoid membrane lipids on the structure and function of the plant photosystem II core complex.Planta · 2014Article
- A bioinspired redox relay that mimics radical interactions of the Tyr-His pairs of photosystem II.Nature chemistry · 2014Article
- Hydrogen tunneling in enzymes and biomimetic models.Chemical reviews · 2014Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
In this article, progress in understanding proton coupled electron transfer (PCET) in Photosystem II is reviewed. Changes in acidity/basicity may accompany oxidation/reduction reactions in biological catalysis. Alterations in the proton transfer pathway can then be used to alter the rates of the electron transfer reactions. Studies of the bioenergetic complexes have played a central role in advancing our understanding of PCET. Because oxidation of the tyrosine results in deprotonation of the phenolic oxygen, redox active tyrosines are involved in PCET reactions in several enzymes. This review focuses on PCET involving the redox active tyrosines in Photosystem II. Photosystem II catalyzes the light-driven oxidation of water and reduction of plastoquinone. Photosystem II provides a paradigm for the study of redox active tyrosines, because this photosynthetic reaction center contains two tyrosines with different roles in catalysis. The tyrosines, YZ and YD, exhibit differences in kinetics and midpoint potentials, and these differences may be due to noncovalent interactions with the protein environment. Here, studies of YD and YZ and relevant model compounds are described.
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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.