ArticleThe journal of physical chemistry letters2012
Proton Coupled Electron Transfer and Redox Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II.
Article in The journal of physical chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 46 citations in OpenAlex.
- Asymmetric Connectivity Between Redox-Active Tyrosines and Reaction-Center Chlorophylls in Photosystem II.Plants (Basel, Switzerland) · 2026Article
- Long-Distance Charge Transport between Cytochrome c and Complex III is Mediated by Protons and Reactive Oxygen Species.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Structure of a ribonucleotide reductase R2 protein radical.Science (New York, N.Y.) · 2023Article
- Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48.The journal of physical chemistry. B · 2023Article
- Roles of High-valent Hemes and pH Dependence in Halite Decomposition Catalyzed by Chlorite Dismutase fromACS catalysis · 2022Article
- Substituent Effects on Photochemistry of Anthracene-Phenol-Pyridine Triads Revealed by Multireference Calculations.Journal of the American Chemical Society · 2020Article
- Detection, identification, and quantification of oxidative protein modifications.The Journal of biological chemistry · 2019Review
- Specific metallo-protein interactions and antimicrobial activity in Histatin-5, an intrinsically disordered salivary peptide.Scientific reports · 2019Article
- Structure and Function of Tryptophan-Tyrosine Dyads in Biomimetic β Hairpins.The journal of physical chemistry. B · 2019Article
- Activationless Multiple-Site Concerted Proton-Electron Tunneling.Journal of the American Chemical Society · 2018Article
- Calcium, conformational selection, and redox-active tyrosine YZ in the photosynthetic oxygen-evolving cluster.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A tyrosine-tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette.Nature communications · 2015Article
- A bioinspired redox relay that mimics radical interactions of the Tyr-His pairs of photosystem II.Nature chemistry · 2014Article
- Biochemistry and theory of proton-coupled electron transfer.Chemical reviews · 2014Review
- Use of electron paramagnetic resonance to solve biochemical problems.Biochemistry · 2013Review
- Redox-linked conformational control of proton-coupled electron transfer: Y122 in the ribonucleotide reductase β2 subunit.The journal of physical chemistry. B · 2013Article
- Redox-linked changes to the hydrogen-bonding network of ribonucleotide reductase β2.Journal of the American Chemical Society · 2013Article
- Assembly and properties of heterobimetallic Co(II/III)/Ca(II) complexes with aquo and hydroxo ligands.Journal of the American Chemical Society · 2012Article
- Molecular mechanisms for generating transmembrane proton gradients.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Proton coupled electron transfer (PCET) reactions are important in many biological processes. Tyrosine oxidation/reduction can play a critical role in facilitating these reactions. Two examples are photosystem II (PSII) and ribonucleotide reductase (RNR). RNR is essential in DNA synthesis in all organisms. In E. coli RNR, a tyrosyl radical, Y122(•), is required as a radical initiator. Photosystem II (PSII) generates molecular oxygen from water. In PSII, an essential tyrosyl radical, YZ(•), oxidizes the oxygen evolving center. However, the mechanisms, by which the extraordinary oxidizing power of the tyrosyl radical is controlled, are not well understood. This is due to the difficulty in acquiring high-resolution structural information about the radical state. Spectroscopic approaches, such as EPR and UV resonance Raman (UVRR), can give new information. Here, we discuss EPR studies of PCET and the PSII YZ radical. We also present UVRR results, which support the conclusion that Y122 undergoes an alteration in ring and backbone dihedral angle when it is oxidized. This conformational change results in a loss of hydrogen bonding to the phenolic oxygen. Our analysis suggests that access of water is an important factor in determining tyrosyl radical lifetime and function. TOC graphic.
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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.