ArticleBiochemistry2013
Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
- Switching the proton-coupled electron transfer mechanism for non-canonical tyrosine residues in aChemical science · 2024Article
- Study and design of amino acid-based radical enzymes using unnatural amino acids.RSC chemical biology · 2023Article
- Selective incorporation of 5-hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase.Protein science : a publication of the Protein Society · 2023Article
- Development of a single cultureJournal of fluorine chemistry · 2022Article
- Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.Annual review of biophysics · 2022Review
- 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
- Structure and Function of Tryptophan-Tyrosine Dyads in Biomimetic β Hairpins.The journal of physical chemistry. B · 2019Article
- Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase.Journal of the American Chemical Society · 2018Article
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm.Biochemistry · 2018Article
- Rapid measurement of long-range distances in proteins by multidimensionalJournal of biomolecular NMR · 2018Article
- Pourbaix Diagram, Proton-Coupled Electron Transfer, and Decay Kinetics of a Protein Tryptophan Radical: Comparing the Redox Properties of WJournal of the American Chemical Society · 2018Article
- Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.Journal of the American Chemical Society · 2017Article
- Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.Biochemistry · 2017Article
- A >200 meV Uphill Thermodynamic Landscape for Radical Transport in Escherichia coli Ribonucleotide Reductase Determined Using Fluorotyrosine-Substituted Enzymes.Journal of the American Chemical Society · 2016Article
- Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.Journal of the American Chemical Society · 2016Article
- Designed metalloprotein stabilizes a semiquinone radical.Nature chemistry · 2016Article
- Charge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase.Journal of the American Chemical Society · 2016Article
- Direct Interfacial YChemical science · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The reversible Y-O•/Y-OH redox properties of the α3Y model protein allow access to the electrochemical and thermodynamic properties of 3,5-difluorotyrosine. The unnatural amino acid has been incorporated at position 32, the dedicated radical site in α3Y, by in vivo nonsense codon suppression. Incorporation of 3,5-difluorotyrosine gives rise to very minor structural changes in the protein scaffold at pH values below the apparent pK (8.0±0.1) of the unnatural residue. Square-wave voltammetry on α3(3,5)F2Y provides an E°'(Y-O•/Y-OH) of 1026±4 mV versus the normal hydrogen electrode (pH 5.70±0.02) and shows that the fluoro substitutions lower the E°' by -30±3 mV. These results illustrate the utility of combining the optimized α3Y tyrosine radical system with in vivo nonsense codon suppression to obtain the formal reduction potential of an unnatural aromatic residue residing within a well-structured protein. It is further observed that the protein E°' values differ significantly from peak potentials derived from irreversible voltammograms of the corresponding aqueous species. This is notable because solution potentials have been the main thermodynamic data available for amino acid radicals. The findings in this paper are discussed relative to recent mechanistic studies of the multistep radical-transfer process in Escherichia coli ribonucleotide reductase site-specifically labeled with unnatural tyrosine residues.
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