ReviewAnnual review of biophysics2022
Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.
Review in Annual review of biophysics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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
14 citing papers in PubMed, 15 citations in OpenAlex.
- Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductaseProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Hole migration in cytochrome P450.QRB discovery · 2026Article
- Antioxidant activity at the molecular level: exploring ways of action and computational tools to investigate them.Chemical science · 2025Review
- Hydroxyl Radical-π Interaction in a Single Crystal.JACS Au · 2025Article
- The Influence of pH on Long-Range Electron Transfer and Proton-Coupled Electron Transfer in Ruthenium-Modified Azurin.Molecules (Basel, Switzerland) · 2025Article
- Hydrogen production by a fullyDalton transactions (Cambridge, England : 2003) · 2024Article
- Proton-Coupled Electron Transfer upon Oxidation of Tyrosine in a De Novo Protein: Analysis of Proton Acceptor Candidates.Biochemistry · 2024Article
- Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).Nature communications · 2024Article
- Switching the proton-coupled electron transfer mechanism for non-canonical tyrosine residues in aChemical science · 2024Article
- Understanding the initial events of the oxidative damage and protection mechanisms of the AA9 lytic polysaccharide monooxygenase family.Chemical 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
- Proximal Methionine Amino Acid Residue Affects the Properties of Redox-Active Tryptophan in an Artificial Model Protein.ACS omega · 2023Article
- Probing the Role of Cysteine Thiyl Radicals in Biology: Eminently Dangerous, Difficult to Scavenge.Antioxidants (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Some oxidoreductase enzymes use redox-active tyrosine, tryptophan, cysteine, and/or glycine residues as one-electron, high-potential redox (radical) cofactors. Amino-acid radical cofactors typically perform one of four tasks-they work in concert with a metallocofactor to carry out a multielectron redox process, serve as storage sites for oxidizing equivalents, activate the substrate molecules, or move oxidizing equivalents over long distances. It is challenging to experimentally resolve the thermodynamic and kinetic redox properties of a single-amino-acid residue. The inherently reactive and highly oxidizing properties of amino-acid radicals increase the experimental barriers further still. This review describes a family of stable and well-structured model proteins that was made specifically to study tyrosine and tryptophan oxidation-reduction. The so-called α
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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.