ArticleJournal of the American Chemical Society2017
Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
27 citing papers in PubMed, 41 citations in OpenAlex.
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- Proton-Coupled Electron Transfer upon Oxidation of Tyrosine in a De Novo Protein: Analysis of Proton Acceptor Candidates.Biochemistry · 2024Article
- Hydrogen production by a fullyDalton transactions (Cambridge, England : 2003) · 2024Article
- Switching the proton-coupled electron transfer mechanism for non-canonical tyrosine residues in aChemical science · 2024Article
- An Investigation of the Influence of Tyrosine Local Interactions on Electron Hopping in a Model Protein.Molecules (Basel, Switzerland) · 2024Article
- Study and design of amino acid-based radical enzymes using unnatural amino acids.RSC chemical biology · 2023Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Selective incorporation of 5-hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase.Protein science : a publication of the Protein Society · 2023Article
- Article
- Kinetic model for reversible radical transfer in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Use of Noncanonical Tyrosine Analogues to Probe Control of Radical Intermediates during Endoperoxide Installation by Verruculogen Synthase (FtmOx1).ACS catalysis · 2022Article
- Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.Annual review of biophysics · 2022Review
- Glutamate Mediates Proton-Coupled Electron Transfer Between Tyrosines 730 and 731 inJournal of the American Chemical Society · 2021Article
- Computing Proton-Coupled Redox Potentials of Fluorotyrosines in a Protein Environment.The journal of physical chemistry. B · 2021Article
- Proton-Coupled Electron Transfer from Tyrosine in the Interior of aJournal of the American Chemical Society · 2020Article
- Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.Annual review of biochemistry · 2020Review
- Salvianolic Acid B in Microemulsion Formulation Provided Sufficient Hydration for Dry Skin and Ameliorated the Severity of Imiquimod-Induced Psoriasis-Like Dermatitis in Mice.Pharmaceutics · 2020Article
- Selenocysteine Substitution in a Class I Ribonucleotide Reductase.Biochemistry · 2019Article
- Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping.Journal of the American Chemical Society · 2019Article
- A Quick and Colorful Method to Measure Low-Level Contaminations of Paramagnetic NiMethods in enzymology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Redox-active tyrosines (Ys) play essential roles in enzymes involved in primary metabolism including energy transduction and deoxynucleotide production catalyzed by ribonucleotide reductases (RNRs). Thermodynamic characterization of Ys in solution and in proteins remains a challenge due to the high reduction potentials involved and the reactive nature of the radical state. The structurally characterized α
Indexed as
Identifiers
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.