ArticleJournal of the American Chemical Society2017
Evidence for a Di-μ-oxo Diamond Core in the Mn(IV)/Fe(IV) Activation Intermediate of Ribonucleotide Reductase from Chlamydia trachomatis.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 34 citations in OpenAlex.
- Selective isotope labeling probes the chemical capacity and reaction mechanism of a heterobimetallic Mn/Fe protein.Journal of inorganic biochemistry · 2025Article
- Design and characterization of a tunable open TEJournal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Structural Elucidation of the Reduced Mn(III)/Fe(III) Intermediate of the Radical-Initiating Metallocofactor inBiochemistry · 2025Article
- Accessing a synthetic FeChemical science · 2024Article
- Resonant Excitation Unlocks Chemical Selectivity of Platinum Lβ Valence-to-Core X-ray Emission Spectra.Inorganic chemistry · 2023Article
- Coordination Number in High-Spin-Low-Spin Equilibrium in Cluster Models of the SJournal of the American Chemical Society · 2023Article
- Determination of the iron(IV) local spin states of the Q intermediate of soluble methane monooxygenase by Kβ X-ray emission spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Spontaneous Formation of an Fe/Mn Diamond Core: Models for the Fe/Mn Sites in Class 1c Ribonucleotide Reductases.Inorganic chemistry · 2021Article
- Stepwise assembly of heterobimetallic complexes: synthesis, structure, and physical properties.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Quantification of Ni-N-O Bond Angles and NO Activation by X-ray Emission Spectroscopy.Inorganic chemistry · 2021Article
- The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein.Journal of the American Chemical Society · 2020Article
- Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins.The Journal of biological chemistry · 2019Article
- High-Resolution Extended X-ray Absorption Fine Structure Analysis Provides Evidence for a Longer Fe···Fe Distance in the Q Intermediate of Methane Monooxygenase.Journal of the American Chemical Society · 2018Article
- Article
- Two-Color Valence-to-Core X-ray Emission Spectroscopy Tracks Cofactor Protonation State in a Class I Ribonucleotide Reductase.Angewandte Chemie (International ed. in English) · 2018Article
- Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by Its Dimanganese Cofactor.Biochemistry · 2018Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Involvement of high-valent manganese-oxo intermediates in oxidation reactions: realisation in nature, nano and molecular systems.Nano convergence · 2018Review
- Oxoiron(IV) complexes as synthons for the assembly of heterobimetallic centers such as the Fe/Mn active site of Class Ic ribonucleotide reductases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
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6 authors at 1 institution in 1 country.
Funding
Abstract
High-valent iron and manganese complexes effect some of the most challenging biochemical reactions known, including hydrocarbon and water oxidations associated with the global carbon cycle and oxygenic photosynthesis, respectively. Their extreme reactivity presents an impediment to structural characterization, but their biological importance and potential chemical utility have, nevertheless, motivated extensive efforts toward that end. Several such intermediates accumulate during activation of class I ribonucleotide reductase (RNR) β subunits, which self-assemble dimetal cofactors with stable one-electron oxidants that serve to initiate the enzyme's free-radical mechanism. In the class I-c β subunit from Chlamydia trachomatis, a heterodinuclear Mn(II)/Fe(II) complex reacts with dioxygen to form a Mn(IV)/Fe(IV) intermediate, which undergoes reduction of the iron site to produce the active Mn(IV)/Fe(III) cofactor. Herein, we assess the structure of the Mn(IV)/Fe(IV) activation intermediate using Fe- and Mn-edge extended X-ray absorption fine structure (EXAFS) analysis and multifrequency pulse electron paramagnetic resonance (EPR) spectroscopy. The EXAFS results reveal a metal-metal vector of 2.74-2.75 Å and an intense light-atom (C/N/O) scattering interaction 1.8 Å from the Fe. Pulse EPR data reveal an exchangeable deuterium hyperfine coupling of strength |T| = 0.7 MHz, but no stronger couplings. The results suggest that the intermediate possesses a di-μ-oxo diamond core structure with a terminal hydroxide ligand to the Mn(IV).
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