ArticleJournal of the American Chemical Society2011
Electrochemical and structural properties of a protein system designed to generate tyrosine Pourbaix diagrams.
Article in Journal of the American Chemical Society, 2011. 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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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.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- The Influence of pH on Long-Range Electron Transfer and Proton-Coupled Electron Transfer in Ruthenium-Modified Azurin.Molecules (Basel, Switzerland) · 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
- 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
- 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
- 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
- A Quick and Colorful Method to Measure Low-Level Contaminations of Paramagnetic NiMethods in enzymology · 2019Article
- 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
- Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.Journal of the American Chemical Society · 2017Article
- Proton-Coupled Electron Transfer in Organic Synthesis: Fundamentals, Applications, and Opportunities.Topics in current chemistry (Cham) · 2016Review
- Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Moving protons and electrons in biomimetic systems.Biochemistry · 2015Review
- 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
- Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.Biochemistry · 2013Article
- Electron flow through nitrotyrosinate in Pseudomonas aeruginosa azurin.Journal of the American Chemical Society · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
This report describes a model protein specifically tailored to electrochemically study the reduction potential of protein tyrosine radicals as a function of pH. The model system is based on the 67-residue α(3)Y three-helix bundle. α(3)Y contains a single buried tyrosine at position 32 and displays structural properties inherent to a protein. The present report presents differential pulse voltammograms obtained from α(3)Y at both acidic (pH 5.6) and alkaline (pH 8.3) conditions. The observed Faradaic response is uniquely associated with Y32, as shown by site-directed mutagenesis. This is the first time voltammetry is successfully applied to detect a redox-active tyrosine residing in a structured protein environment. Tyrosine is a proton-coupled electron-transfer cofactor making voltammetry-based pH titrations a central experimental approach. A second set of experiments was performed to demonstrate that pH-dependent studies can be conducted on the redox-active tyrosine without introducing large-scale structural changes in the protein scaffold. α(3)Y was re-engineered with the specific aim to place the imidazole group of a histidine close to the Y32 phenol ring. α(3)Y-K29H and α(3)Y-K36H each contain a histidine residue whose protonation perturbs the fluorescence of Y32. We show that these variants are stable and well-folded proteins whose helical content, tertiary structure, solution aggregation state, and solvent-sequestered position of Y32 remain pH insensitive across a range of at least 3-4 pH units. These results confirm that the local environment of Y32 can be altered and the resulting radical site studied by voltammetry over a broad pH range without interference from long-range structural effects.
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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.