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<sup>19</sup>F Electron-Nuclear Double Resonance Reveals Interaction between Redox-Active Tyrosines across the α/β Interface of <i>E. coli</i> Ribonucleotide Reductase

Andreas Meyer, Annemarie Kehl, Chang Cui, Fehmke A. K. Reichardt, Fabian Hecker, Lisa-Marie Funk, Manas K. Ghosh, Kuan‐Ting Pan, Henning Urlaub, Kai Tittmann, JoAnne Stubbe, Marina Bennati

2022Journal of the American Chemical Society37 citationsDOIOpen Access PDF

Abstract

. The results highlight the important role of state-of-the-art EPR spectroscopy to decipher this mechanism.

Topics & Concepts

Ribonucleotide reductaseChemistryElectron nuclear double resonanceElectron paramagnetic resonanceElectron transferRibonucleotideDeoxyribonucleotidesCrystallographyResonance (particle physics)StereochemistryElectron acceptorCofactorPulsed EPRAcceptorMutantElectron transport chainPhotochemistryNucleotideEnzymeNuclear magnetic resonanceBiochemistryAtomic physicsProtein subunitRadiologyCondensed matter physicsMedicinePhysicsGeneMagnetic resonance imagingSpin echoElectron Spin Resonance StudiesMetal-Catalyzed Oxygenation MechanismsLanthanide and Transition Metal Complexes
<sup>19</sup>F Electron-Nuclear Double Resonance Reveals Interaction between Redox-Active Tyrosines across the α/β Interface of <i>E. coli</i> Ribonucleotide Reductase | Litcius