ArticleJournal of the American Chemical Society2022
Pulsed Multifrequency Electron Paramagnetic Resonance Spectroscopy Reveals Key Branch Points for One- vs Two-Electron Reactivity in Mn/Fe Proteins.
Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- A protein-based model of carbon monoxide dehydrogenase exhibits tunable covalency across cluster oxidation and ligand-bound states.Chemical science · 2026Article
- The Factors Governing Metal Dependence of an Emergent Superfamily of Bimetallic Oxygenases.Journal of the American Chemical Society · 2026Article
- Unsymmetric bimetallic centres in metalloproteins and synthetic models.Nature reviews. Chemistry · 2026Review
- Selective isotope labeling probes the chemical capacity and reaction mechanism of a heterobimetallic Mn/Fe protein.Journal of inorganic biochemistry · 2025Article
- Structural Elucidation of the Reduced Mn(III)/Fe(III) Intermediate of the Radical-Initiating Metallocofactor inBiochemistry · 2025Article
- Accessing a synthetic FeChemical science · 2024Article
- Bioinformatic Discovery of a Cambialistic Monooxygenase.Journal of the American Chemical Society · 2024Article
- Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.Journal of the American Chemical Society · 2023Article
- Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
5 authors.
Funding
Abstract
Traditionally, the ferritin-like superfamily of proteins was thought to exclusively use a diiron active site in catalyzing a diverse array of oxygen-dependent reactions. In recent years, novel redox-active cofactors featuring heterobimetallic Mn/Fe active sites have been discovered in both the radical-generating R2 subunit of class Ic (R2c) ribonucleotide reductases (RNRs) and the related R2-like ligand-binding oxidases (R2lox). However, the protein-specific factors that differentiate the radical reactivity of R2c from the C-H activation reactions of R2lox remain unknown. In this work, multifrequency pulsed electron paramagnetic resonance (EPR) spectroscopy and ligand hyperfine techniques in conjunction with broken-symmetry density functional theory calculations are used to characterize the molecular and electronic structures of two EPR-active intermediates trapped during aerobic assembly of the R2lox Mn/Fe cofactor. A Mn
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