ArticleJournal of the American Chemical Society2015
Hydrogen bond network between amino acid radical intermediates on the proton-coupled electron transfer pathway of E. coli α2 ribonucleotide reductase.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 67 citations in OpenAlex.
- Asymmetric Connectivity Between Redox-Active Tyrosines and Reaction-Center Chlorophylls in Photosystem II.Plants (Basel, Switzerland) · 2026Article
- Structural Elucidation of the Reduced Mn(III)/Fe(III) Intermediate of the Radical-Initiating Metallocofactor inBiochemistry · 2025Article
- Hydrogen Tunneling and Conformational Motions in Nonadiabatic Proton-Coupled Electron Transfer between Interfacial Tyrosines in Ribonucleotide Reductase.Journal of the American Chemical Society · 2025Article
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Direct Proton-Coupled Electron Transfer between Interfacial Tyrosines in Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Proton transfer reactions: From photochemistry to biochemistry and bioenergetics.BBA advances · 2023Article
- Article
- Kinetic model for reversible radical transfer in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Role of Water in Proton-Coupled Electron Transfer between Tyrosine and Cysteine in Ribonucleotide Reductase.Journal of the American Chemical Society · 2022Article
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 2021Article
- In-Cell Characterization of the Stable Tyrosyl Radical in E. coli Ribonucleotide Reductase Using Advanced EPR Spectroscopy.Angewandte Chemie (International ed. in English) · 2021Article
- Diversity of structures and functions of oxo-bridged non-heme diiron proteins.Archives of biochemistry and biophysics · 2021Review
- Statistical analysis of ENDOR spectra.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Detection of Water Molecules on the Radical Transfer Pathway of Ribonucleotide Reductase byJournal of the American Chemical Society · 2021Article
- Glutamate Mediates Proton-Coupled Electron Transfer Between Tyrosines 730 and 731 inJournal of the American Chemical Society · 2021Article
- Determining electron-nucleus distances and Fermi contact couplings from ENDOR spectra.Physical chemistry chemical physics : PCCP · 2021Article
- Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2021Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides in all organisms. In all Class Ia RNRs, initiation of nucleotide diphosphate (NDP) reduction requires a reversible oxidation over 35 Å by a tyrosyl radical (Y122•, Escherichia coli) in subunit β of a cysteine (C439) in the active site of subunit α. This radical transfer (RT) occurs by a specific pathway involving redox active tyrosines (Y122 ⇆ Y356 in β to Y731 ⇆ Y730 ⇆ C439 in α); each oxidation necessitates loss of a proton coupled to loss of an electron (PCET). To study these steps, 3-aminotyrosine was site-specifically incorporated in place of Y356-β, Y731- and Y730-α, and each protein was incubated with the appropriate second subunit β(α), CDP and effector ATP to trap an amino tyrosyl radical (NH2Y•) in the active α2β2 complex. High-frequency (263 GHz) pulse electron paramagnetic resonance (EPR) of the NH2Y•s reported the gx values with unprecedented resolution and revealed strong electrostatic effects caused by the protein environment. (2)H electron-nuclear double resonance (ENDOR) spectroscopy accompanied by quantum chemical calculations provided spectroscopic evidence for hydrogen bond interactions at the radical sites, i.e., two exchangeable H bonds to NH2Y730•, one to NH2Y731• and none to NH2Y356•. Similar experiments with double mutants α-NH2Y730/C439A and α-NH2Y731/Y730F allowed assignment of the H bonding partner(s) to a pathway residue(s) providing direct evidence for colinear PCET within α. The implications of these observations for the PCET process within α and at the interface are discussed.
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