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Function of the Diiron Cluster ofEscherichia coliClass Ia Ribonucleotide Reductase in Proton-Coupled Electron Transfer
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/9783527612192.ch21openalex-snapshot
Adenosylcobalamin‐Dependent Ribonucleotide Reductases: Still Amazing but No Longer Confusing
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Identification of the stable free radical tyrosine residue in ribonucleotide reductase.
inferredcites →https://doi.org/10.1002/jcc.10189openalex-snapshot
Energies, structures, and electronic properties of molecules in solution with the C‐PCM solvation model
inferredcites →https://doi.org/10.1002/jcc.10318openalex-snapshot
An improvement of the resolution of the identity approximation for the formation of the Coulomb matrix
inferredcites →https://doi.org/10.1007/s00775-011-0755-1openalex-snapshot
Oxygen cleavage with manganese and iron in ribonucleotide reductase from Chlamydia trachomatis
inferredcites →https://doi.org/10.1016/0005-2728(70)90060-5openalex-snapshot
The state of copper in stellacyanin and laccase from the lacquer tree Rhus vernicifera
inferredcites →https://doi.org/10.1016/0022-2364(75)90045-1openalex-snapshot
EPR signal intensity and powder shapes: A reexamination
inferredcites →https://doi.org/10.1016/j.chemphys.2008.10.036openalex-snapshot
Efficient, approximate and parallel Hartree–Fock and hybrid DFT calculations. A ‘chain-of-spheres’ algorithm for the Hartree–Fock exchange
inferredcites →https://doi.org/10.1016/s0021-9258(17)32750-3openalex-snapshot
Nature of the free radical in ribonucleotide reductase from Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(17)33753-5openalex-snapshot
Active site of ribonucleoside diphosphate reductase from Escherichia coli. Inactivation of the enzyme by 2'-substituted ribonucleoside diphosphates.
inferredcites →https://doi.org/10.1016/s0021-9258(17)37999-1openalex-snapshot
The tyrosine free radical in ribonucleotide reductase from Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(18)33031-xopenalex-snapshot
Mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3'-C--H bond cleavage.
inferredcites →https://doi.org/10.1016/s0021-9258(18)42322-8openalex-snapshot
Escherichia coli ribonucleotide reductase. Radical susceptibility to hydroxyurea is dependent on the regulatory state of the enzyme.
inferredcites →https://doi.org/10.1016/s0021-9258(18)83154-4openalex-snapshot
Mössbauer and EPR studies of the binuclear iron center in ribonucleotide reductase from Escherichia coli
inferredcites →https://doi.org/10.1016/s0021-9258(19)43313-9openalex-snapshot
Iron and Free Radical in Ribonucleotide Reductase
inferredcites →https://doi.org/10.1016/s0021-9258(19)45166-1openalex-snapshot
Electron Spin Resonance of the Iron-containing Protein B2 from Ribonucleotide Reductase
inferredcites →https://doi.org/10.1016/s0021-9258(19)70598-5openalex-snapshot
On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3'-C–H bond cleavage.
inferredcites →https://doi.org/10.1021/bi00135a009openalex-snapshot
Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction
inferredcites →https://doi.org/10.1021/bi00155a031openalex-snapshot
Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity
inferredcites →https://doi.org/10.1021/bi00210a026openalex-snapshot
Alternative model for mechanism-based inhibition of Escherichia coli ribonucleotide reductase by 2'-azido-2'-deoxyuridine 5'-diphosphate
inferredcites →https://doi.org/10.1021/bi00386a024openalex-snapshot
Products of the inactivation of ribonucleoside diphosphate reductase from Escherichia coli with 2'-azido-2'-deoxyuridine 5'-diphosphate
inferredcites →https://doi.org/10.1021/bi034374ropenalex-snapshot
Pre-Steady-State and Steady-State Kinetic Analysis of E. coli Class I Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/cr00102a002openalex-snapshot
Oxo- and hydroxo-bridged diiron complexes: a chemical perspective on a biological unit
inferredcites →https://doi.org/10.1021/cr020421uopenalex-snapshot
Radical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?
inferredcites →https://doi.org/10.1021/cr9400875openalex-snapshot
Protein Radicals in Enzyme Catalysis
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Protein Radicals in Enzyme Catalysis. [ Chem. Rev. 1998 , 98 , 705−762
inferredcites →https://doi.org/10.1021/ic048609eopenalex-snapshot
Performance of Nonrelativistic and Quasi-Relativistic Hybrid DFT for the Prediction of Electric and Magnetic Hyperfine Parameters in57Fe Mössbauer Spectra
inferredcites →https://doi.org/10.1021/ic801535vopenalex-snapshot
Calibration of Modern Density Functional Theory Methods for the Prediction of 57Fe Mössbauer Isomer Shifts: Meta-GGA and Double-Hybrid Functionals
inferredcites →https://doi.org/10.1021/j100161a081openalex-snapshot
Electrochemical properties of tyrosine phenoxy and tryptophan indolyl radicals in peptides and amino acid analogs
inferredcites →https://doi.org/10.1021/ja00140a003openalex-snapshot
EPR Investigations of the Inactivation of E. coli Ribonucleotide Reductase with 2'-Azido-2'-deoxyuridine 5'-Diphosphate: Evidence for the Involvement of the Thiyl Radical of C225-R1
inferredcites →https://doi.org/10.1021/ja0362095openalex-snapshot
Pulsed ELDOR Spectroscopy Measures the Distance between the Two Tyrosyl Radicals in the R2 Subunit of the E. coli Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja043111xopenalex-snapshot
Structure of the Nitrogen-Centered Radical Formed during Inactivation ofE. coliRibonucleotide Reductase by 2‘-Azido-2‘-deoxyuridine-5‘-diphosphate: Trapping of the 3‘-Ketonucleotide
inferredcites →https://doi.org/10.1021/ja054991yopenalex-snapshot
EPR Distance Measurements Support a Model for Long-Range Radical Initiation in E. coli Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja055927jopenalex-snapshot
pH Rate Profiles of FnY356−R2s (n = 2, 3, 4) in Escherichia coli Ribonucleotide Reductase: Evidence that Y356 Is a Redox-Active Amino Acid along the Radical Propagation Pathway
inferredcites →https://doi.org/10.1021/ja057776qopenalex-snapshot
Site-Specific Replacement of Y 356 with 3,4-Dihydroxyphenylalanine in the β2 Subunit of E. coli Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja0685607openalex-snapshot
Forward and Reverse Electron Transfer with the Y356DOPA-β2 Heterodimer of E. coli Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja076043yopenalex-snapshot
Site-Specific Insertion of 3-Aminotyrosine into Subunit α2 of E. coli Ribonucleotide Reductase: Direct Evidence for Involvement of Y 730 and Y 731 in Radical Propagation
inferredcites →https://doi.org/10.1021/ja076459bopenalex-snapshot
PELDOR Spectroscopy with DOPA-β2 and NH2Y-α2s: Distance Measurements between Residues Involved in the Radical Propagation Pathway of E. coli Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja1069344openalex-snapshot
A Hot Oxidant, 3-NO2Y122 Radical, Unmasks Conformational Gating in Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja207455kopenalex-snapshot
Equilibration of Tyrosyl Radicals (Y356•, Y731•, Y730•) in the Radical Propagation Pathway of the Escherichia coli Class Ia Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja3071682openalex-snapshot
ENDOR Spectroscopy and DFT Calculations: Evidence for the Hydrogen-Bond Network Within α2 in the PCET of E. coli Ribonucleotide Reductase
inferredcites →https://doi.org/10.1021/ja970319sopenalex-snapshot
Differential Iron(II) Affinity of the Sites of the Diiron Cluster in Protein R2 of Escherichia coli Ribonucleotide Reductase: Tracking the Individual Sites through the O2 Activation Sequence
inferredcites →https://doi.org/10.1021/ja9826845openalex-snapshot
Differing Roles for the Diiron Clusters of Ribonucleotide Reductase from Aerobically Grown Escherichia c oli in the Generation of the Y122 Radical
inferredcites →https://doi.org/10.1021/jp9827835openalex-snapshot
Hydrogen Atom Transfer in Ribonucleotide Reductase (RNR)
inferredcites →https://doi.org/10.1038/370533a0openalex-snapshot
Structure of ribonucleotide reductase protein R1
inferredcites →https://doi.org/10.1038/nsb774openalex-snapshot
The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer
inferredcites →https://doi.org/10.1039/c1dt10950bopenalex-snapshot
Mössbauer properties of the diferric cluster and the differential iron(ii)-binding affinity of the iron sites in protein R2 of class Ia Escherichia coli ribonucleotide reductase: a DFT/electrostatics study
inferredcites →https://doi.org/10.1039/p29930000799openalex-snapshot
COSMO: a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
inferredcites →https://doi.org/10.1063/1.2761879openalex-snapshot
On the calculation of Mössbauer isomer shift
inferredcites →https://doi.org/10.1063/1.438955openalex-snapshot
Self-consistent molecular orbital methods. XX. A basis set for correlated wave functions
inferredcites →https://doi.org/10.1063/1.440939openalex-snapshot
Valence bond description of antiferromagnetic coupling in transition metal dimers
inferredcites →https://doi.org/10.1063/1.464913openalex-snapshot
Density-functional thermochemistry. III. The role of exact exchange
inferredcites →https://doi.org/10.1073/pnas.0536684100openalex-snapshot
Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-Å x-ray data
inferredcites →https://doi.org/10.1073/pnas.1112715108openalex-snapshot
Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase
inferredcites →https://doi.org/10.1074/jbc.271.34.20655openalex-snapshot
Two Conserved Tyrosine Residues in Protein R1 Participate in an Intermolecular Electron Transfer in Ribonucleotide Reductase
inferredcites →https://doi.org/10.1074/jbc.273.33.21003openalex-snapshot
Preserved Catalytic Activity in an Engineered Ribonucleotide Reductase R2 Protein with a Nonphysiological Radical Transfer Pathway
inferredcites →https://doi.org/10.1098/rstb.2006.1874openalex-snapshot
Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology
inferredcites →https://doi.org/10.1103/physrevb.37.785openalex-snapshot
Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
inferredcites →https://doi.org/10.1126/science.1650033openalex-snapshot
Mechanism of Assembly of the Tyrosyl Radical-Dinuclear Iron Cluster Cofactor of Ribonucleotide Reductase
inferredcites →https://doi.org/10.1126/science.271.5248.477openalex-snapshot
Thiyl Radicals in Ribonucleotide Reductases
inferredcites →https://doi.org/10.1126/science.283.5407.1499openalex-snapshot
A Glycyl Radical Site in the Crystal Structure of a Class III Ribonucleotide Reductase
inferredcites →https://doi.org/10.1146/annurev.biochem.75.103004.142443openalex-snapshot
Ribonucleotide Reductases
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Structural Insights into the Initiation of Free Radical Formation in the Class Ib Ribonucleotide Reductases in Mycobacteria
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Structural Insights into the Initiation of Free Radical Formation in the Class Ib Ribonucleotide Reductases in Mycobacteria
inferred← citeshttps://doi.org/10.1002/9781118925645.ch2openalex-snapshot
The Essential Role of Iron in Biology
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Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H2O2 but Slowly with O2
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Direct Observation of Ultrafast Proton Rocking in the BLUF Domain
inferred← citeshttps://doi.org/10.1002/anie.202015964openalex-snapshot
Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H2O2 but Slowly with O2
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Direct Observation of Ultrafast Proton Rocking in the BLUF Domain
inferred← citeshttps://doi.org/10.1007/s00775-016-1357-8openalex-snapshot
Mono- and binuclear non-heme iron chemistry from a theoretical perspective
inferred← citeshttps://doi.org/10.1016/b978-0-08-102688-5.00059-3openalex-snapshot
Diiron Enzyme Structure and Catalysis
inferred← citeshttps://doi.org/10.1016/b978-0-12-409547-2.14865-6openalex-snapshot
Structure-Function Relationships in Assembly of the Radical-Initiating Cofactors of Class Ia–e Ribonucleotide Reductases
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Design, engineering, and characterization of switchable artificial metalloproteins (swArMs)
inferred← citeshttps://doi.org/10.1016/j.bbabio.2014.09.003openalex-snapshot
Reaction dynamics and proton coupled electron transfer: Studies of tyrosine-based charge transfer in natural and biomimetic systems
inferred← citeshttps://doi.org/10.1016/j.ccr.2019.213176openalex-snapshot
O2 and H2O2 activations at dinuclear Mn and Fe active sites
inferred← citeshttps://doi.org/10.1016/j.crstbi.2024.100157openalex-snapshot
Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases in Mycobacteria
inferred← citeshttps://doi.org/10.1016/j.jbc.2021.101137openalex-snapshot
The periodic table of ribonucleotide reductases
inferred← citeshttps://doi.org/10.1016/j.wasman.2025.114925openalex-snapshot
Unraveling the electron hopping mechanism in biochar-enhanced syntrophic acetate oxidation for methane production
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Electron flow through biological molecules: does hole hopping protect proteins from oxidative damage?
inferred← citeshttps://doi.org/10.1021/acs.biochem.1c00779openalex-snapshot
Metal Dependence and Functional Diversity of Type I Cas3 Nucleases
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Vibrio cholerae V-cGAP3 Is an HD-GYP Phosphodiesterase with a Metal Tunable Substrate Selectivity
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Structural Elucidation of the Reduced Mn(III)/Fe(III) Intermediate of the Radical-Initiating Metallocofactor in Chlamydia trachomatis Ribonucleotide Reductase
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Biochemical Studies of a Cyanobacterial Halogenase Support the Involvement of a Dimetal Cofactor
inferred← citeshttps://doi.org/10.1021/acs.biochem.5c00316openalex-snapshot
A Structurally Divergent Class Ia Ribonucleotide Reductase from a Tick-Borne Pathogen
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Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00462openalex-snapshot
Spectroscopic Evidence for a H Bond Network at Y356 Located at the Subunit Interface of Active E. coli Ribonucleotide Reductase
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Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm
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Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by Its Dimanganese Cofactor
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Theoretical Insights into the Generation Mechanism of the Tyr122 Radical Catalyzed by Intermediate X in Class Ia Ribonucleotide Reductase
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Carboxylate Shift Dynamics in Biomimetic Co2(μ–OH)2 Complexes
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Detection of Catalytically Linked Conformational Changes in Wild-Type Class Ia Ribonucleotide Reductase Using Reaction-Induced FTIR Spectroscopy
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Elementary Reactions in the Functional Triads of the Blue-Light Photoreceptor BLUF Domain
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A Proton Wire Mediates Proton Coupled Electron Transfer from Hydroxyurea and Other Hydroxamic Acids to Tyrosyl Radical in Class Ia Ribonucleotide Reductase
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E. coli Ribonucleotide Reductase β2 Subunit Inactivation by Triapine Occurs through Binding of a Triapine–Fe(II) Adduct
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Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase
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Electron Flow through Metalloproteins
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Biochemistry and Theory of Proton-Coupled Electron Transfer
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Geometric and Electronic Structure of the Mn(IV)Fe(III) Cofactor in Class Ic Ribonucleotide Reductase: Correlation to the Class Ia Binuclear Non-Heme Iron Enzyme
inferred← citeshttps://doi.org/10.1021/ja507313wopenalex-snapshot
Kinetics of Hydrogen Atom Abstraction from Substrate by an Active Site Thiyl Radical in Ribonucleotide Reductase
inferred← citeshttps://doi.org/10.1021/ja510513zopenalex-snapshot
Hydrogen Bond Network between Amino Acid Radical Intermediates on the Proton-Coupled Electron Transfer Pathway of E. coli α2 Ribonucleotide Reductase
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Conformational Motions and Water Networks at the α/β Interface in E. coli Ribonucleotide Reductase
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Theoretical Study of Shallow Distance Dependence of Proton-Coupled Electron Transfer in Oligoproline Peptides
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Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase
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Engineering a Conformationally Switchable Artificial Metalloprotein
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Reverse Electron Transfer Completes the Catalytic Cycle in a 2,3,5-Trifluorotyrosine-Substituted Ribonucleotide Reductase
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Charge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase
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Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase
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Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase
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Conformational control over proton-coupled electron transfer in metalloenzymes
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A platform for distributed production of synthetic nitrated proteins in live bacteria
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Direct interfacial Y 731 oxidation in α 2 by a photoβ 2 subunit of E. coli class Ia ribonucleotide reductase
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Radical transfer in E. coli ribonucleotide reductase: a NH 2 Y 731 /R 411 A-α mutant unmasks a new conformation of the pathway residue 731
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Functional and protective hole hopping in metalloenzymes
inferred← citeshttps://doi.org/10.1042/ebc20160072openalex-snapshot
Long-range proton-coupled electron transfer in the Escherichia coli class Ia ribonucleotide reductase
inferred← citeshttps://doi.org/10.1073/pnas.1811993115openalex-snapshot
Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical
inferred← citeshttps://doi.org/10.1073/pnas.2202022119openalex-snapshot
Kinetic model for reversible radical transfer in ribonucleotide reductase
inferred← citeshttps://doi.org/10.1073/pnas.2417157121openalex-snapshot
2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor N 3 CDP
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Glutamate 52-β at the α/β subunit interface of Escherichia coli class Ia ribonucleotide reductase is essential for conformational gating of radical transfer
inferred← citeshttps://doi.org/10.1098/rsta.2014.0178openalex-snapshot
Could tyrosine and tryptophan serve multiple roles in biological redox processes?
inferred← citeshttps://doi.org/10.1126/science.aba6794openalex-snapshot
Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex
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Structure of a ribonucleotide reductase R2 protein radical
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Conformational Control over Proton-Coupled Electron Transfer in Metalloenzymes
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Conformational Control over Proton-Coupled Electron Transfer in Metalloenzymes
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Hydrogen Bonds and Electrostatic Environment of Radical Intermediates in Ribonucleotide Reductase Ia
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