ArticleJournal of the American Chemical Society2009
Proton-coupled electron transfer in photosystem II: proton inventory of a redox active tyrosine.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 67 citations in OpenAlex.
- Regulation of light energy conversion between linear and cyclic electron flow within photosystem II controlled by the plastoquinone/quinol redox poise.Photosynthesis research · 2023Article
- Proton Conduction at High Temperature in High-Symmetry Hydrogen-Bonded Molecular Crystals of RuChemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Non-coordinated and Hydrogen Bonded Phenolate Anions as One-Electron Reducing Agents.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- One Electron Multiple Proton Transfer in Model Organic Donor-Acceptor Systems: Implications for High Frequency EPR.Applied magnetic resonance · 2020Article
- Anomalous chemically induced electron spin polarization in proton-coupled electron transfer reactions: insight into radical pair dynamics.Chemical science · 2020Article
- Specific metallo-protein interactions and antimicrobial activity in Histatin-5, an intrinsically disordered salivary peptide.Scientific reports · 2019Article
- Insights into the catalytic mechanism of a bacterial hydrolytic dehalogenase that degrades the fungicide chlorothalonil.The Journal of biological chemistry · 2019Article
- Microsolvation of the Redox-Active Tyrosine-D in Photosystem II: Correlation of Energetics with EPR Spectroscopy and Oxidation-Induced Proton Transfer.Journal of the American Chemical Society · 2019Article
- A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Biochemistry · 2016Article
- Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.The Biochemical journal · 2016Article
- A tyrosine-tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette.Nature communications · 2015Article
- Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A bioinspired redox relay that mimics radical interactions of the Tyr-His pairs of photosystem II.Nature chemistry · 2014Article
- Proton-coupled electron transfer: Free radicals under control.Nature chemistry · 2014Article
- Biochemistry and theory of proton-coupled electron transfer.Chemical reviews · 2014Review
- Proton transport facilitating water-oxidation: the role of second sphere ligands surrounding the catalytic metal cluster.Photosynthesis research · 2013Review
- Redox-linked conformational control of proton-coupled electron transfer: Y122 in the ribonucleotide reductase β2 subunit.The journal of physical chemistry. B · 2013Article
- Photochemical Tyrosine Oxidation with a Hydrogen-Bonded Proton Acceptor by Bidirectional Proton-Coupled Electron Transfer.Chemical science · 2012Article
- Reductive activation of the heme iron-nitrosyl intermediate in the reaction mechanism of cytochrome c nitrite reductase: a theoretical study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Proton Coupled Electron Transfer and Redox Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II.The journal of physical chemistry letters · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Photosystem II (PSII) catalyzes the light driven oxidation of water and the reduction of plastoquinone. PSII is a multisubunit membrane protein; the D1 and D2 polypeptides form the heterodimeric core of the PSII complex. Water oxidation occurs at a manganese-containing oxygen evolving complex (OEC). PSII contains two redox active tyrosines, Y(Z) and Y(D), which form the neutral tyrosyl radicals, Y(z)(*) and Y(D)(*). Y(D) has been assigned as tyrosine 160 in the D2 polypeptide through isotopic labeling and site-directed mutagenesis. Whereas Y(D) is not directly involved in the oxidation of water, it has been implicated in the formation and stabilization of the OEC. PSII structures have shown Y(D) to be within hydrogen-bonding distance of histidine 189 in the D2 polypeptide. Spectroscopic studies have suggested that a proton is transferred between Y(D) and histidine 189 when Y(D) is oxidized and reduced. In our previous work, we used (2)H(2)O solvent exchange to demonstrate that the mechanism of Y(D) proton-coupled electron transfer (PCET) differs at high and low pH. In this article, we utilize the proton inventory technique to obtain more information concerning PCET mechanism at high pH. The hypercurvature of the proton inventory data provides evidence for the existence of multiple, proton-donation pathways to Y(D)(*). In addition, at least one of these pathways must involve the transfer of more than one proton.
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