l-Tryptophan Radical Cation Electron Spin Resonance Studies: Connecting Solution-Derived Hyperfine Coupling Constants with Protein Spectral Interpretations
Author:
Affiliation:
1. Laboratory of Pharmacology and Chemistry, National Institute of Environmental Health Sciences, National Institutes of Health, P.O. Box 12233, Research Triangle Park, North Carolina 27709
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja0780277
Reference39 articles.
1. Properties of Photogenerated Tryptophan and Tyrosyl Radicals in Structurally Characterized Proteins Containing Rhenium(I) Tricarbonyl Diimines
2. Spectroscopy and Reactivity of a Photogenerated Tryptophan Radical in a Structurally Defined Protein Environment
3. Electron-Transfer Chemistry of Ru−Linker−(Heme)-Modified Myoglobin: Rapid Intraprotein Reduction of a Photogenerated Porphyrin Cation Radical
4. Compound ES of Cytochrome c Peroxidase Contains a Trp .pi.-Cation Radical: Characterization by Continuous Wave and Pulsed Q-Band External Nuclear Double Resonance Spectroscopy
5. Reaction of Bovine Cytochrome c Oxidase with Hydrogen Peroxide Produces a Tryptophan Cation Radical and a Porphyrin Cation Radical
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