ArticleJournal of the American Chemical Society2011
Hydrogen bonding of tryptophan radicals revealed by EPR at 700 GHz.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 57 citations in OpenAlex.
- Machine Learning IsotropicJournal of chemical theory and computation · 2024Article
- Proximal Methionine Amino Acid Residue Affects the Properties of Redox-Active Tryptophan in an Artificial Model Protein.ACS omega · 2023Article
- Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.Biochemistry · 2023Article
- Selective incorporation of 5-hydroxytryptophan blocks long range electron transfer in oxalate decarboxylase.Protein science : a publication of the Protein Society · 2023Article
- Pulsed Multifrequency Electron Paramagnetic Resonance Spectroscopy Reveals Key Branch Points for One- vs Two-Electron Reactivity in Mn/Fe Proteins.Journal of the American Chemical Society · 2022Article
- Unique Biradical Intermediate in the Mechanism of the Heme Enzyme Chlorite Dismutase.ACS catalysis · 2021Article
- Trapping a cross-linked lysine-tryptophan radical in the catalytic cycle of the radical SAM enzyme SuiB.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure and Function of Tryptophan-Tyrosine Dyads in Biomimetic β Hairpins.The journal of physical chemistry. B · 2019Article
- Photonic band-gap resonators for high-field/high-frequency EPR of microliter-volume liquid aqueous samples.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- High-Frequency/High-Field Electron Paramagnetic Resonance and Theoretical Studies of Tryptophan-Based Radicals.The journal of physical chemistry. A · 2018Article
- A Radical Intermediate in Bacillus subtilis QueE during Turnover with the Substrate Analogue 6-Carboxypterin.Journal of the American Chemical Society · 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
- Efficient methylation of C2 in l-tryptophan by the cobalamin-dependent radicalThe Journal of biological chemistry · 2017Article
- The Color of Cation-π Interactions: Subtleties of Amine-Tryptophan Interaction Energetics Allow for Radical-like Visible Absorbance and Fluorescence.Journal of the American Chemical Society · 2017Article
- Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I.Biochimica et biophysica acta · 2016Review
- Proton-Coupled Electron Transfer in Organic Synthesis: Fundamentals, Applications, and Opportunities.Topics in current chemistry (Cham) · 2016Review
- A tyrosine-tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette.Nature communications · 2015Article
- The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction.Nature communications · 2015Article
- Photogeneration and Quenching of Tryptophan Radical in Azurin.The journal of physical chemistry. B · 2015Article
- High-frequency and high-field electron paramagnetic resonance (HFEPR): a new spectroscopic tool for bioinorganic chemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
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7 authors at 4 institutions in 1 country.
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Abstract
Redox-active tryptophans are important in biological electron transfer and redox biochemistry. Proteins can tune the electron transfer kinetics and redox potentials of tryptophan via control of the protonation state and the hydrogen-bond strength. We examine the local environment of two neutral tryptophan radicals (Trp108 on the solvent-exposed surface and Trp48 buried in the hydrophobic core) in two azurin variants. Ultrahigh-field EPR spectroscopy at 700 GHz and 25 T allowed complete resolution of all of the principal components of the g tensors of the two radicals and revealed significant differences in the g tensor anisotropies. The spectra together with (2)H ENDOR spectra and supporting DFT calculations show that the g tensor anisotropy is directly diagnostic of the presence or absence as well as the strength of a hydrogen bond to the indole nitrogen. The approach is a powerful one for identifying and characterizing hydrogen bonds that are critical in the regulation of tryptophan-assisted electron transfer and tryptophan-mediated redox chemistry in proteins.
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