ArticleBiochemistry2013
Reversible phenol oxidation and reduction in the structurally well-defined 2-Mercaptophenol-α₃C protein.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Label-free optical detection of protein acetylation using UV-vis charge transfer spectra.Chemical science · 2026Article
- Hydroxyl Radical-π Interaction in a Single Crystal.JACS Au · 2025Article
- 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
- Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.Annual review of biophysics · 2022Review
- Proton-Coupled Electron Transfer from Tyrosine in the Interior of aJournal of the American Chemical Society · 2020Article
- Uno Ferro, a de novo Designed Protein, Binds Transition Metals with High Affinity and Stabilizes Semiquinone Radical Anion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- A Quick and Colorful Method to Measure Low-Level Contaminations of Paramagnetic NiMethods in enzymology · 2019Article
- 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
- 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
- Near UV-Visible electronic absorption originating from charged amino acids in a monomeric protein.Chemical science · 2017Article
- Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.Journal of the American Chemical Society · 2017Article
- Designed metalloprotein stabilizes a semiquinone radical.Nature chemistry · 2016Article
- Electrochemical Interrogation of G3-Poly(propylene thiophenoimine) Dendritic Star Polymer in Phenanthrene Sensing.Sensors (Basel, Switzerland) · 2015Article
- Photochemical tyrosine oxidation in the structurally well-defined α3Y protein: proton-coupled electron transfer and a long-lived tyrosine radical.Journal of the American Chemical Society · 2014Article
- An Anisotropic Coarse-Grained Model for Proteins Based On Gay-Berne and Electric Multipole Potentials.Journal of chemical theory and computation · 2014Article
- Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.Biochemistry · 2013Article
- Iron(IV)hydroxide pK(a) and the role of thiolate ligation in C-H bond activation by cytochrome P450.Science (New York, N.Y.) · 2013Article
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Abstract
2-Mercaptophenol-α₃C serves as a biomimetic model for enzymes that use tyrosine residues in redox catalysis and multistep electron transfer. This model protein was tailored for electrochemical studies of phenol oxidation and reduction with specific emphasis on the redox-driven protonic reactions occurring at the phenol oxygen. This protein contains a covalently modified 2-mercaptophenol-cysteine residue. The radical site and the phenol compound were specifically chosen to bury the phenol OH group inside the protein. A solution nuclear magnetic resonance structural analysis (i) demonstrates that the synthetic 2-mercaptophenol-α₃C model protein behaves structurally as a natural protein, (ii) confirms the design of the radical site, (iii) reveals that the ligated phenol forms an interhelical hydrogen bond to glutamate 13 (phenol oxygen-carboxyl oxygen distance of 3.2 ± 0.5 Å), and (iv) suggests a proton-transfer pathway from the buried phenol OH (average solvent accessible surface area of 3 ± 5%) via glutamate 13 (average solvent accessible surface area of the carboxyl oxygens of 37 ± 18%) to the bulk solvent. A square-wave voltammetry analysis of 2-mercaptophenol-α₃C further demonstrates that (v) the phenol oxidation-reduction cycle is reversible, (vi) formal phenol reduction potentials can be obtained, and (vii) the phenol-O(•) state is long-lived with an estimated lifetime of ≥180 millisecond. These properties make 2-mercaptophenol-α₃C a unique system for characterizing phenol-based proton-coupled electron transfer in a low-dielectric and structured protein environment.
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