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Three-dimensional structure of the free radical protein of ribonucleotide reductase
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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/j.1460-2075.1983.tb01684.xopenalex-snapshot
DNA sequence homology between two co‐linear loci on the HSV genome which have different transforming abilities.
inferredcites →https://doi.org/10.1002/j.1460-2075.1986.tb04287.xopenalex-snapshot
Using known substructures in protein model building and crystallography.
inferredcites →https://doi.org/10.1002/j.1460-2075.1986.tb04460.xopenalex-snapshot
The bacteriophage T4 gene for the small subunit of ribonucleotide reductase contains an intron.
inferredcites →https://doi.org/10.1002/j.1460-2075.1986.tb04461.xopenalex-snapshot
Identification of the stable free radical tyrosine residue in ribonucleotide reductase.
inferredcites →https://doi.org/10.1002/j.1460-2075.1989.tb08383.xopenalex-snapshot
Molecular cloning and expression of the functional gene encoding the M2 subunit of mouse ribonucleotide reductase: a new dominant marker gene.
inferredcites →https://doi.org/10.1016/0006-291x(90)92098-kopenalex-snapshot
Activation of the iron-containing B2 protein of ribonucleotide reductase by hydrogen peroxide
inferredcites →https://doi.org/10.1016/0014-5793(87)80214-4openalex-snapshot
Characterization of the free radical in a plant ribonucleotide reductase
inferredcites →https://doi.org/10.1016/0014-5793(89)81666-7openalex-snapshot
New crystal forms of the small subunit of ribonucleotide reductase from Escherichia coli
inferredcites →https://doi.org/10.1016/0022-2836(79)90308-5openalex-snapshot
Gene duplications in the structural evolution of chymotrypsin
inferredcites →https://doi.org/10.1016/0022-2836(82)90452-1openalex-snapshot
Crystallographic refinement and atomic models of two different forms of citrate synthase at 2·7 and 1·7 Å resolution
inferredcites →https://doi.org/10.1016/0022-2836(87)90124-0openalex-snapshot
Structure of myohemerythrin in the azidomet state at resolution
inferredcites →https://doi.org/10.1016/0022-2836(89)90499-3openalex-snapshot
Pseudo 2-fold symmetry in the copper-binding domain of arthropodan haemocyanins
inferredcites →https://doi.org/10.1016/0042-6822(88)90421-7openalex-snapshot
Oligopeptides inhibit the ribonucleotide reductase of herpes simplex virus by causing subunit separation
inferredcites →https://doi.org/10.1016/0076-6879(85)15009-3openalex-snapshot
Resolution of phase ambiguity in macromolecular crystallography
inferredcites →https://doi.org/10.1016/0076-6879(85)15014-7openalex-snapshot
Interactive computer graphics: FRODO
inferredcites →https://doi.org/10.1016/0968-0004(87)90163-0openalex-snapshot
Transferrins: insights into structure and function from studies on lactoferrin
inferredcites →https://doi.org/10.1016/s0021-9258(17)36209-9openalex-snapshot
The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.
inferredcites →https://doi.org/10.1016/s0021-9258(18)37554-9openalex-snapshot
Mechanism of inhibition of herpes simplex virus (HSV) ribonucleotide reductase by a nonapeptide corresponding to the carboxyl terminus of its subunit 2. Specific binding of a photoaffinity analog, [4′- azido-Phe6] HSV H2-6(6-15), to subunit 1.
inferredcites →https://doi.org/10.1016/s0021-9258(18)45356-2openalex-snapshot
NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)47996-3openalex-snapshot
Half-site reactivity of the tyrosyl radical of ribonucleotide reductase from Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(18)60509-5openalex-snapshot
Enzymatic Regulation of the Radical Content of the Small Subunit of Escherichia coli Ribonucleotide Reductase Involving Reduction of Its Redox Centers
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(18)83205-7openalex-snapshot
Resonance Raman evidence for tyrosine involvement in the radical site of galactose oxidase
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)77903-4openalex-snapshot
Radical formation in the dimeric small subunit of ribonucleotide reductase requires only one tyrosine 122.
inferredcites →https://doi.org/10.1021/bi00389a017openalex-snapshot
Extended x-ray absorption fine structure studies on the iron-containing subunit of ribonucleotide reductase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi00391a049openalex-snapshot
Magnetic interaction between the tyrosyl free radical and the antiferromagnetically coupled iron center in ribonucleotide reductase
inferredcites →https://doi.org/10.1021/bi00426a001openalex-snapshot
Directed mutagenesis indicates that the donor to P 680+ in photosystem II is tyrosine-161 of the D1 polypeptide
inferredcites →https://doi.org/10.1021/bi00430a074openalex-snapshot
Resonance Raman spectroscopy of ribonucleotide reductase. Evidence for a deprotonated tyrosyl radical and photochemistry of the binuclear iron center
inferredcites →https://doi.org/10.1021/bi00432a039openalex-snapshot
Reduced forms of the iron-containing small subunit of ribonucleotide reductase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi00530a017openalex-snapshot
Raman spectral evidence for a .mu.-oxo bridge in the binuclear iron center of ribonucleotide reductase
inferredcites →https://doi.org/10.1021/ja00203a002openalex-snapshot
An ENDOR study of the tyrosyl free radical in ribonucleotide reductase from Escherichia coli
inferredcites →https://doi.org/10.1021/ja00281a077openalex-snapshot
EXAFS studies of the B2 subunit of the ribonucleotide reductase from E. coli
inferredcites →https://doi.org/10.1038/257028a0openalex-snapshot
Three-dimensional model of purple membrane obtained by electron microscopy
inferredcites →https://doi.org/10.1038/318618a0openalex-snapshot
Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
inferredcites →https://doi.org/10.1073/pnas.81.14.4294openalex-snapshot
Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon.
inferredcites →https://doi.org/10.1073/pnas.82.3.713openalex-snapshot
Active site structures of deoxyhemerythrin and oxyhemerythrin.
inferredcites →https://doi.org/10.1083/jcb.100.6.1968openalex-snapshot
The small subunit of ribonucleotide reductase is encoded by one of the most abundant translationally regulated maternal RNAs in clam and sea urchin eggs.
inferredcites →https://doi.org/10.1093/nar/12.12.5087openalex-snapshot
Homology between two EBV early genes and HSV ribonudeotide reductase and 38K genes
inferredcites →https://doi.org/10.1093/protein/2.8.589openalex-snapshot
Conservation of residue interactions in a family of Ca-binding proteins
inferredcites →https://doi.org/10.1099/0022-1317-67-9-1759openalex-snapshot
The Complete DNA Sequence of Varicella-Zoster Virus
inferredcites →https://doi.org/10.1107/s0021889887086783openalex-snapshot
A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector
inferredcites →https://doi.org/10.1107/s0108767383001592openalex-snapshot
Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions
inferredcites →https://doi.org/10.1107/s0567739476001691openalex-snapshot
Methods and programs for direct-space exploitation of geometric redundancies
inferredcites →https://doi.org/10.1111/j.1432-1033.1969.tb00639.xopenalex-snapshot
Spectrum and Iron Content of Protein B2 from Ribonucleoside Diphosphate Reductase
inferredcites →https://doi.org/10.1111/j.1432-1033.1988.tb13792.xopenalex-snapshot
Higher oxidation states of prostaglandin H synthase
inferredcites →https://doi.org/10.1126/science.235.4787.458openalex-snapshot
Crystallographic R Factor Refinement by Molecular Dynamics
inferredcites →https://doi.org/10.1128/jvi.57.3.802-808.1986openalex-snapshot
Herpes simplex virus specifies two subunits of ribonucleotide reductase encoded by 3'-coterminal transcripts
inferredcites →https://doi.org/10.1128/jvi.62.2.519-527.1988openalex-snapshot
Vaccinia virus-encoded ribonucleotide reductase: sequence conservation of the gene for the small subunit and its amplification in hydroxyurea-resistant mutants
inferredcites →https://doi.org/10.1128/jvi.63.9.3769-3776.1989openalex-snapshot
Herpes simplex virus ribonucleotide reductase: expression in Escherichia coli and purification to homogeneity of a tyrosyl free radical-containing, enzymatically active form of the 38-kilodalton subunit
inferredcites →https://doi.org/10.1128/mcb.6.10.3433openalex-snapshot
Isolation and Characterization of Expressible cDNA Clones Encoding the M1 and M2 Subunits of Mouse Ribonucleotide Reductase
inferredcites →https://doi.org/10.1128/mcb.7.10.3673openalex-snapshot
Identification of the Gene for the Yeast Ribonucleotide Reductase Small Subunit and Its Inducibility by Methyl Methanesulfonate
inferredcites →https://doi.org/10.1128/mcb.7.8.2783openalex-snapshot
Identification and Isolation of the Gene Encoding the Small Subunit of Ribonucleotide Reductase from Saccharomyces cerevisiae: DNA Damage-Inducible Gene Required for Mitotic Viability
inferredcites →https://doi.org/10.1146/annurev.bi.58.070189.001353openalex-snapshot
PROTEIN RADICAL INVOLVEMENT IN BIOLOGICAL CATALYSIS?
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4796736openalex-extracted
Structural Insights into the Initiation of Free Radical Formation in the Class Ib Ribonucleotide Reductases in Mycobacteria
inferred← citeshttps://doi.org/10.2139/ssrn.4808936openalex-extracted
Structural Insights into the Initiation of Free Radical Formation in the Class Ib Ribonucleotide Reductases in Mycobacteria
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Structural and Functional Investigations on Diiron Complexes: Catalase-Like Activity and Mechanistic Studies on the Formation of (μ-Peroxo)diiron(III) Adducts
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The active site of the plant alternative oxidase: structural and mechanistic considerations
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Δ9Stearoyl‐Acyl Carrier Protein Desaturase
inferred← citeshttps://doi.org/10.1002/0470028637.met229openalex-snapshot
Ribonucleotide Reductase: Recent Advances
inferred← citeshttps://doi.org/10.1002/1521-3757(20010803)113:15<2860::aid-ange2860>3.0.co;2-2openalex-snapshot
Aktivierung von Disauerstoff und Hydroxylierung von Methan durch lösliche Methan-Monooxygenase: eine Geschichte von zwei Eisenatomen und drei Proteinen
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Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins
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Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.
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Real‐time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer
inferred← citeshttps://doi.org/10.1002/9780470015902.a0000567.pub3openalex-snapshot
Ribonucleotide Reduction
inferred← citeshttps://doi.org/10.1002/9780470123119.ch4openalex-snapshot
The Redox Centers of Ribonucleotide Reductase of Escherichia coli
inferred← citeshttps://doi.org/10.1002/9780470166390.ch3openalex-snapshot
Dinuclear Iron‐ and Manganese‐Oxo Sites in Biology
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Slow Proton‐Transfer Reactions in Organometallic and Bioinorganic Chemistry
inferred← citeshttps://doi.org/10.1002/9781118165850.ch11openalex-snapshot
Structural and Functional Aspects of Metal Binding Sites in Natural and Designed Metalloproteins
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0578openalex-snapshot
Ribonucleotide Reductase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0580openalex-snapshot
Δ9Stearoyl‐Acyl Carrier Protein Desaturase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0656openalex-snapshot
Ribonucleotide Reductase: Recent Advances
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2329openalex-snapshot
Dinuclear Iron Cluster‐Containing Oxygenase CmlA
inferred← citeshttps://doi.org/10.1002/9781444345988.ch16openalex-snapshot
Transfer of Free Radicals between Proteins and Membrane Lipids: Implications for Aquatic Biology
inferred← citeshttps://doi.org/10.1002/9783527611546.ch17openalex-snapshot
The Relation between Hydrogen Atom Transfer and Proton‐coupled Electron Transfer in Model Systems
inferred← citeshttps://doi.org/10.1002/9783527613700.ch10openalex-snapshot
The anaerobic ribonucleotide reductase fromEscherichia coli
inferred← citeshttps://doi.org/10.1002/9783527613700.ch16openalex-snapshot
Intermediates in oxygen activation reactions of diiron enzymes
inferred← citeshttps://doi.org/10.1002/9783527613700.ch20openalex-snapshot
Structural versatility of proteins containing rubredoxin‐type centers
inferred← citeshttps://doi.org/10.1002/9783527618248.ch41openalex-snapshot
Electron Transfer in Hydrogen‐Bonded Donor‐Acceptor Supramolecules
inferred← citeshttps://doi.org/10.1002/9783527619450.ch9openalex-snapshot
C‐H Transformation at Unfunctionalized Alkanes
inferred← citeshttps://doi.org/10.1002/9783527629213.ch18openalex-snapshot
Computational Electronic Structure of Spin‐Coupled Diiron‐Oxo Proteins
inferred← citeshttps://doi.org/10.1002/9783527636730openalex-snapshot
Peptide Drug Discovery and Development
inferred← citeshttps://doi.org/10.1002/9783527636730.ch1openalex-snapshot
Peptides as Leads for Drug Discovery
inferred← citeshttps://doi.org/10.1002/ange.19911030916openalex-snapshot
Reduktion der kleinen Untereinheit der Ribonucleotid‐Reductase mit Diimid: Beweise für die Bildung eines gemischtvalenten FeIIFeIII‐Zentrums
inferred← citeshttps://doi.org/10.1002/ange.19921041142openalex-snapshot
Multifeld‐Sättigungsmagnetisierungsmessungen an oxidierter und reduzierter Ribonucleotid‐Reduktase aus Escherichia coli
inferred← citeshttps://doi.org/10.1002/ange.19931050932openalex-snapshot
Molekulare Erkennung im Innern einer starren Wirtverbindung: Strukturänderungen in carboxylatoverbrückten Dimetall(II)‐Komplexen beim Wechsel von sterischer Hinderung zu Wasserstoffbrückenbindungen
inferred← citeshttps://doi.org/10.1002/ange.19941060817openalex-snapshot
Ein gemischtvalenter, unsymmetrischer FeIIFEIII‐Komplex mit einem terminalen Phenolatoliganden als Modell für das aktive Zentrum violetter saurer Phosphatasen
inferred← citeshttps://doi.org/10.1002/ange.19941061541openalex-snapshot
Carboxylatoeisen( II )‐Aggregate: ein neuer Fe‐Komplex mit dreizähliger Symmetrie
inferred← citeshttps://doi.org/10.1002/ange.19961082024openalex-snapshot
Durch einen μ‐Oxodieisen(III)‐Komplex katalysierte Hydroxylierung eines Arylliganden mit H2O2 und O2
inferred← citeshttps://doi.org/10.1002/ange.200352368openalex-snapshot
How Single and Bifurcated Hydrogen Bonds Influence Proton‐Migration Rate Constants, Redox, and Electronic Properties of Phenoxyl Radicals
inferred← citeshttps://doi.org/10.1002/ange.201812343openalex-snapshot
Origin of Nitric Oxide Reduction Activity in Flavo–Diiron NO Reductase: Key Roles of the Second Coordination Sphere
inferred← citeshttps://doi.org/10.1002/ange.202015964openalex-snapshot
Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H2O2 but Slowly with O2
inferred← citeshttps://doi.org/10.1002/ange.202524825openalex-snapshot
50 Years of Giese Reaction – a Personal View
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Single‐Atom‐Modulated Reactive Oxygen Species Generation and Network Crosslinking in Porphyrin‐Based Metallacages for Selective Photocatalysis
inferred← citeshttps://doi.org/10.1002/anie.199111351openalex-snapshot
Reduction of the Small Subunit of Ribonucleotide Reductase by Diimide: Evidence for the Formation of the Mixed‐Valence Fe II Fe III center
inferred← citeshttps://doi.org/10.1002/anie.199215131openalex-snapshot
Multifield Saturation Magnetization Measurements of Oxidized and Reduced Ribonucleotide Reductase from Escherichia coli
inferred← citeshttps://doi.org/10.1002/anie.199313211openalex-snapshot
Molecular Recognition within a Rigid Host: Structural Changes Induced in μ‐Carboxylato Dimetal( II ) Complexes by Replacing Steric Repulsions with Hydrogen Bonds
inferred← citeshttps://doi.org/10.1002/anie.199408871openalex-snapshot
A Mixed‐Valent, Unsymmetrical FeIIFeIII Complex with a Terminal Phenolato Ligand as a Model for the Active Site of Purple Acid Phosphatases
inferred← citeshttps://doi.org/10.1002/anie.199416601openalex-snapshot
Carboxylatoiron( II ) Aggregates: A Novel Fe Complex with Threefold Symmetry
inferred← citeshttps://doi.org/10.1002/anie.199623531openalex-snapshot
Aromatic Hydroxylation by H2O2 and O2 Catalyzed by a μ‐Oxo Diiron( III ) Complex
inferred← citeshttps://doi.org/10.1002/anie.200352368openalex-snapshot
How Single and Bifurcated Hydrogen Bonds Influence Proton‐Migration Rate Constants, Redox, and Electronic Properties of Phenoxyl Radicals
inferred← citeshttps://doi.org/10.1002/anie.201812343openalex-snapshot
Origin of Nitric Oxide Reduction Activity in Flavo–Diiron NO Reductase: Key Roles of the Second Coordination Sphere
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
inferred← citeshttps://doi.org/10.1002/anie.202525287openalex-snapshot
Single‐Atom‐Modulated Reactive Oxygen Species Generation and Network Crosslinking in Porphyrin‐Based Metallacages for Selective Photocatalysis
inferred← citeshttps://doi.org/10.1002/aoc.1199openalex-snapshot
Synthesis, magnetic property and DNA cleavage behavior of a new dialkoxo‐bridged diiron(III) complex
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A radical approach to enzyme catalysis
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Unsymmetric Dinucleating Ligands for Metallobiosite Modelling
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Trapping Transient Protein Species by Genetic Code Expansion
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Substrate Specificity of B12‐Depedent Ribonucleotide Reductases: Biotechnology and Metabolic Implications
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ProPhenol Derived Ligands to Simultaneously Coordinate a Main‐Group Metal and a Transition Metal: Application to a Zn−Cu Catalyzed Reaction
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QM/MM Unlocks The Catalytic Mechanism of YtfE: The Structural Reorganization of The Active Site Enables Nitrite‐to‐NO Conversion
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ChemInform Abstract: A Mechanistic Analysis of C—O Bond Cleavage Events with a Comparison to 3,6‐Dideoxysugar Formation
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Quantum Chemical Studies of Radical-Containing Enzymes
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Electronic and Structural Heterogeneity in the Diiron Center of Sulerythrin: Insights From Hybrid QM/MM Calculations
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Galactose Oxidase Models: Creation and Modification of Proton Transfer Coupled to Copper(II) Coordination Processes in Pro‐Phenoxyl Ligands
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A Discrete μ4‐Oxido Tetranuclear Iron(III) Cluster
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Artificial Diiron Enzymes with a De Novo Designed Four‐Helix Bundle Structure
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A Dinucleating Ligand System with Varying Terminal Donors to Mimic Diiron Active Sites
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Crystal structure of delta9 stearoyl‐acyl carrier protein desaturase from castor seed and its relationship to other di‐iron proteins.
inferred← citeshttps://doi.org/10.1002/jcc.10389openalex-snapshot
Class I ribonucleotide reductase revisited: The effect of removing a proton on Glu441
inferred← citeshttps://doi.org/10.1002/jcc.1157openalex-snapshot
Computational studies of reaction mechanisms of methane monooxygenase and ribonucleotide reductase
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Ribonucleotide activation by enzyme ribonucleotide reductase: Understanding the role of the enzyme
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Das Resistenzproblem bei der Therapie von Mykobakteriosen: Neue Experimentelle Wirkstoffe und Kombinationen für die Therapie der Tuberkulose und der Lepra
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Crystal structure of the hydroxylase component of methane monooxygenase fromMethylosinus trichosporiumOB3b
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Studies of the zein‐like α‐prolamins based on an analysis of amino acid sequences: Implications for their evolution and three‐dimensional structure
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Ribonucleotide reductase of herpesviruses
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S‐Denitrosylation by the C‐Terminal Swinging Arm of R1 Subunit: A Novel Mechanism to Restore Ribonucleotide Reductase Activity
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Synthesis, Structure, and Spectroscopic Properties of a Dinuclear FeIII(μ2‐O)FeIII Complex Using a Strongly Electron‐Donating Ligand: Implications for the Generation of New High‐Valent Species
inferred← citeshttps://doi.org/10.1002/zaac.200300246openalex-snapshot
Trinuclear Mixed‐Valent MnII/MnIV/MnII Complexes — Structure and Magnetic Behavior
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Synthesis and Crystal Structure of a New Dinuclear Iron(III) Complex: [Fe2O(PhCO2)2(2,2′‐bpy)2(N3)2]·H2O
inferred← citeshttps://doi.org/10.1002/zaac.201500551openalex-snapshot
Magnetic and Spectroscopic Study on a New Asymmetric Mixed‐valence Mn2(II,III) Coordination Compound
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Generation and Electron Paramagnetic Resonance Spin Trapping Detection of Thiyl Radicals in Model Proteins and in the R1 Subunit of Escherichia coli Ribonucleotide Reductase
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New Paramagnetic Species Formed at the Expense of the Transient Tyrosyl Radical in Mutant Protein R2 F208Y ofEscherichia coliRibonucleotide Reductase
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Biochemical and Spectroscopic Characterization of Overexpressed Fuscoredoxin from Escherichia coli
inferred← citeshttps://doi.org/10.1006/jmbi.1997.0970openalex-snapshot
Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution 1 1Edited by R. Huber
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1189openalex-snapshot
Crystal structure of the bacteriochlorophyll a protein from Chlorobium tepidum 1 1Edited by R. Huber
inferred← citeshttps://doi.org/10.1006/jmbi.2001.4513openalex-snapshot
Evolution of function in protein superfamilies, from a structural perspective 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.2001.5061openalex-snapshot
High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin
inferred← citeshttps://doi.org/10.1007/0-306-46828-x_12openalex-snapshot
Ribonucleotide Reductase A Virtual Playground for Electron Transfer Reactions
inferred← citeshttps://doi.org/10.1007/0-306-48205-3_8openalex-snapshot
The Use of Cyanobacteria in the Study of the Structure and Function of Photosystem II
inferred← citeshttps://doi.org/10.1007/1-4020-3286-2_14openalex-snapshot
Ab Initio Molecular Dynamics Simulations of Biologically Relevant Systems
inferred← citeshttps://doi.org/10.1007/1-4020-4254-x_10openalex-snapshot
The Redox-Active Tyrosines YZ and YD
inferred← citeshttps://doi.org/10.1007/10721878_6openalex-snapshot
Degradation and Transformation of Organic Fluorine Compounds
inferred← citeshttps://doi.org/10.1007/3-540-30439-8_80openalex-snapshot
Ribonucleoside-diphosphate reductase
inferred← citeshttps://doi.org/10.1007/3-540-62870-3_5openalex-snapshot
Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism
inferred← citeshttps://doi.org/10.1007/3418_2019_29openalex-snapshot
Oxygen Effect in Heteromultimetallic Catalysis: Oxygen-Bridged Catalysts for Olefin Polymerization Process
inferred← citeshttps://doi.org/10.1007/978-0-387-84856-3_7openalex-snapshot
Binuclear Non-Heme Iron Enzymes
inferred← citeshttps://doi.org/10.1007/978-1-4020-9956-4_2openalex-snapshot
The Oniom Method and its Applications to Enzymatic Reactions
inferred← citeshttps://doi.org/10.1007/978-1-4613-0365-7_35openalex-snapshot
Model Systems and Structure, Function and Reactivity Relationships in Transition Metal-Containing Biopolymers
inferred← citeshttps://doi.org/10.1007/978-1-4613-0669-6_35openalex-snapshot
Model Systems and Structure, Function and Reactivity Relationships in Transition Metal-Containing Biopolymers
inferred← citeshttps://doi.org/10.1007/978-1-4613-1185-0_7openalex-snapshot
Utilization of Nitric Oxide as a Paramagnetic Probe of the Molecular Oxygen Binding Site of Metalloenzymes
inferred← citeshttps://doi.org/10.1007/978-1-4613-9783-0_5openalex-snapshot
Oxygen Activation at Nonheme Iron Centers
inferred← citeshttps://doi.org/10.1007/978-1-4615-2886-9_7openalex-snapshot
NMR of Polymetallic Systems in Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4615-2892-0_2openalex-snapshot
Mössbauer Spectroscopy of Iron Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4757-4379-1_5openalex-snapshot
The use of Very High Frequency EPR (VHF-EPR) in Studies of Radicals and Metal Sites in Proteins and Small Inorganic Models
inferred← citeshttps://doi.org/10.1007/978-1-4757-9235-5_4openalex-snapshot
Oxygenation by Methane Monooxygenase: Oxygen Activation and Component Interactions
inferred← citeshttps://doi.org/10.1007/978-1-4757-9235-5_5openalex-snapshot
Structure and Mechanism of Action of the Enzyme(s) Involved in Methane Oxidation
inferred← citeshttps://doi.org/10.1007/978-1-4899-2338-7_3openalex-snapshot
Methane Oxidation by Methanotrophs
inferred← citeshttps://doi.org/10.1007/978-1-4899-2338-7_4openalex-snapshot
The Genetics and Molecular Biology of Obligate Methane-Oxidizing Bacteria
inferred← citeshttps://doi.org/10.1007/978-1-4899-6718-3_10openalex-snapshot
Inactivation of Herpes Simplex Virus Ribonucleotide Reductase by Subunit Association Inhibitors: A Potential Antiviral Strategy
inferred← citeshttps://doi.org/10.1007/978-3-031-00793-4_4openalex-snapshot
Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes
inferred← citeshttps://doi.org/10.1007/978-3-031-52858-3_9openalex-snapshot
Sauerstoffeffekt in heteromultimetallischer Katalyse: Sauerstoffbrückenkatalysatoren für den Olefinpolymerisationsprozess
inferred← citeshttps://doi.org/10.1007/978-3-0348-7784-8_5openalex-snapshot
Current and potential therapies for the treatment of herpesvirus infections
inferred← citeshttps://doi.org/10.1007/978-3-0348-8012-1_8openalex-snapshot
Current and potential therapies for the treatment of herpesvirus infections
inferred← citeshttps://doi.org/10.1007/978-3-0348-8319-1_2openalex-snapshot
Current and potential therapies for the treatment of herpes-virus infections
inferred← citeshttps://doi.org/10.1007/978-3-322-91893-2_7openalex-snapshot
Eisen-Schwefel- und andere Nichthäm-Eisen-Proteine
inferred← citeshttps://doi.org/10.1007/978-3-322-92714-9_7openalex-snapshot
Eisen-Schwefel- und andere Nichthäm-Eisen-Proteine
inferred← citeshttps://doi.org/10.1007/978-3-322-94722-2_7openalex-snapshot
Eisen-Schwefel- und andere Nicht-Hämeisen-Proteine
inferred← citeshttps://doi.org/10.1007/978-3-642-01228-0_14openalex-snapshot
Regulation by Non-Covalent Interactions
inferred← citeshttps://doi.org/10.1007/978-3-642-38111-9_6openalex-snapshot
Hydroxamates as Ribonucleotide Reductase Inhibitors
inferred← citeshttps://doi.org/10.1007/978-3-642-48724-8_1openalex-snapshot
Spin-Labeled Medicines: Enzymes, Biomembranes and Possible Pharmaceuticals. An Overview
inferred← citeshttps://doi.org/10.1007/978-3-642-57942-4_185openalex-snapshot
Ribonucleoside-diphosphate reductase
inferred← citeshttps://doi.org/10.1007/978-3-642-79488-9_10openalex-snapshot
Structure of Ribonucleotide Reductase from Escherichia coli
inferred← citeshttps://doi.org/10.1007/978-3-642-85252-7_18openalex-snapshot
Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins
inferred← citeshttps://doi.org/10.1007/978-3-663-01605-2_7openalex-snapshot
Eisen-Schwefel- und andere Nichthäm-Eisen-Proteine
inferred← citeshttps://doi.org/10.1007/978-4-431-68180-9_13openalex-snapshot
Mutagenesis Studies on the Amino Acid Residues Involved in an Iron-Binding Domain and a Catalytic Site of Human 5-Lipoxygenase
inferred← citeshttps://doi.org/10.1007/978-94-009-0213-8_20openalex-snapshot
Carboxylate Shifts in the Active Site of the Hydroxylase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath)
inferred← citeshttps://doi.org/10.1007/978-94-011-0227-8_8openalex-snapshot
The Use of Cyanobacteria in the Study of the Structure and Function of Photosystem II
inferred← citeshttps://doi.org/10.1007/978-94-011-0255-1_6openalex-snapshot
Mechanistic Studies on the Binuclear Fe Enzymes Ribonucleotide Reductase and Purple Acid Phosphatase
inferred← citeshttps://doi.org/10.1007/978-94-011-0609-2_5openalex-snapshot
Oxygen Activation at Nonheme Iron Centers
inferred← citeshttps://doi.org/10.1007/978-94-011-1474-5_82openalex-snapshot
Synthesis of the zinc complex of Boc-Glu-Thr-Ile-His-OMe: The model peptides for the metal binding sites of ribonucleotide reductase
inferred← citeshttps://doi.org/10.1007/978-94-011-2140-8_7openalex-snapshot
Models for iron biomolecules
inferred← citeshttps://doi.org/10.1007/978-94-011-2140-8_8openalex-snapshot
Iron chelators of clinical significance
inferred← citeshttps://doi.org/10.1007/978-94-011-2290-0_5openalex-snapshot
The metabolism of nucleotides
inferred← citeshttps://doi.org/10.1007/978-94-011-4615-9_17openalex-snapshot
Protein Surface Recognition
inferred← citeshttps://doi.org/10.1007/978-94-011-4818-4_2openalex-snapshot
Insights into the active site of the plant alternative oxidase and its relationship to function
inferred← citeshttps://doi.org/10.1007/978-94-015-8909-3_11openalex-snapshot
Synthesis and Storage of Fatty Acids
inferred← citeshttps://doi.org/10.1007/bf00279553openalex-snapshot
The cell cycle genes cdc22 + and suc22 + of the fission yeast Schizosaccharomyces pombe encode the large and small subunits of ribonucleotide reductase
inferred← citeshttps://doi.org/10.1007/bf00696456openalex-snapshot
Molecular genetics of methane oxidation
inferred← citeshttps://doi.org/10.1007/bf00696461openalex-snapshot
Genetics and biochemistry of phenol degradation byPseudomonas sp. CF600
inferred← citeshttps://doi.org/10.1007/bf02109999openalex-snapshot
Structure-function relationships of the alternative oxidase of plant mitochondria: A model of the active site
inferred← citeshttps://doi.org/10.1007/bf02969446openalex-snapshot
Synthesis, crystal structure of diferrous complex and its reactivity with dioxygen
inferred← citeshttps://doi.org/10.1007/bf03162416openalex-snapshot
High-frequency EPR and ENDOR: Time-domain spectroscopy of ribonucleotide reductase
inferred← citeshttps://doi.org/10.1007/bf03166595openalex-snapshot
Tyrosyl radical, diiron center and enzyme mechanism in ribonucleotide reductase
inferred← citeshttps://doi.org/10.1007/s000180050356openalex-snapshot
Nitric oxide: a radical molecule in quest of free radicals in proteins
inferred← citeshttps://doi.org/10.1007/s00249-005-0026-6openalex-snapshot
Computational studies on class I ribonucleotide reductase: understanding the mechanisms of action and inhibition of a cornerstone enzyme for the treatment of cancer
inferred← citeshttps://doi.org/10.1007/s00253-001-0843-1openalex-snapshot
Biotechnologically relevant enzymes from Thermus thermophilus
inferred← citeshttps://doi.org/10.1007/s00280-008-0890-8openalex-snapshot
A phase I study of Triapine® in combination with doxorubicin in patients with advanced solid tumors
inferred← citeshttps://doi.org/10.1007/s00775-004-0582-8openalex-snapshot
Characterization of NO adducts of the diiron center in protein R2 of Escherichia coli ribonucleotide reductase and site-directed variants; implications for the O2 activation mechanism*
inferred← citeshttps://doi.org/10.1007/s00775-009-0606-5openalex-snapshot
The manganese/iron-carboxylate proteins: what is what, where are they, and what can the sequences tell us?
inferred← citeshttps://doi.org/10.1007/s00775-011-0755-1openalex-snapshot
Oxygen cleavage with manganese and iron in ribonucleotide reductase from Chlamydia trachomatis
inferred← citeshttps://doi.org/10.1007/s00775-014-1136-3openalex-snapshot
Mechanisms of iron mineralization in ferritins: one size does not fit all
inferred← citeshttps://doi.org/10.1007/s00775-014-1140-7openalex-snapshot
Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins
inferred← citeshttps://doi.org/10.1007/s00775-016-1363-xopenalex-snapshot
Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway
inferred← citeshttps://doi.org/10.1007/s00775-016-1425-0openalex-snapshot
Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis
inferred← citeshttps://doi.org/10.1007/s00775-019-01703-zopenalex-snapshot
Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access
inferred← citeshttps://doi.org/10.1007/s10751-017-1452-4openalex-snapshot
Nuclear inelastic scattering at the diiron center of ribonucleotide reductase from Escherichia coli
inferred← citeshttps://doi.org/10.1007/s10822-012-9581-yopenalex-snapshot
Understanding the molecular interactions of different radical scavengers with ribonucleotide reductase M2 (hRRM2) domain: opening the gates and gaining access
inferred← citeshttps://doi.org/10.1007/s11224-025-02496-5openalex-snapshot
Dinuclear oxido-bridged iron(III) complexes containing sulfato ligands
inferred← citeshttps://doi.org/10.1007/s12275-016-5642-6openalex-snapshot
Hydroxylation of methane through component interactions in soluble methane monooxygenases
inferred← citeshttps://doi.org/10.1007/s40487-023-00221-yopenalex-snapshot
Biochemistry—Not Oncogenes—May Demystify and Defeat Cancer
inferred← citeshttps://doi.org/10.1007/s41061-016-0030-6openalex-snapshot
Proton-Coupled Electron Transfer in Organic Synthesis: Fundamentals, Applications, and Opportunities
inferred← citeshttps://doi.org/10.1016/0003-2697(92)90443-bopenalex-snapshot
Monitoring of iron(III) removal from biological sources using a fluorescent siderophore
inferred← citeshttps://doi.org/10.1016/0005-2728(96)00022-9openalex-snapshot
The ferritins: molecular properties, iron storage function and cellular regulation
inferred← citeshttps://doi.org/10.1016/0006-291x(91)91390-xopenalex-snapshot
Inactivation of ribonucleotide reductase by nitric oxide
inferred← citeshttps://doi.org/10.1016/0006-291x(92)91138-gopenalex-snapshot
EPR stopped-flow studies of the reaction of the tyrosyl radical of protein r2 from ribonucleotide reductase with hydroxyurea
inferred← citeshttps://doi.org/10.1016/0006-291x(92)91901-2openalex-snapshot
Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase
inferred← citeshttps://doi.org/10.1016/0006-2952(92)90686-dopenalex-snapshot
Effect of gallium on the tyrosyl radical of the iron-dependent M2 subunit of ribonucleotide reductase
inferred← citeshttps://doi.org/10.1016/0014-5793(92)80417-fopenalex-snapshot
Mechanism of catalysis of Fe(II) oxidation by ferritin H chains
inferred← citeshttps://doi.org/10.1016/0014-5793(92)80690-iopenalex-snapshot
The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase
inferred← citeshttps://doi.org/10.1016/0014-5793(93)81629-eopenalex-snapshot
Crystallization and crystallographic investigations of ribonucleotide reductase protein R1 from Escherichia coli
inferred← citeshttps://doi.org/10.1016/0014-5793(94)00781-0openalex-snapshot
Direct observation of the iron binding sites in a ferritin
inferred← citeshttps://doi.org/10.1016/0014-5793(94)01397-jopenalex-snapshot
Molecular characterization and cell cycle‐regulated expression of a cDNA clone from Arabidopsis thaliana homologous to the small subunit of ribonucleotide reductase
inferred← citeshttps://doi.org/10.1016/0014-5793(95)00196-gopenalex-snapshot
The active site of the cyanide‐resistant oxidase from plant mitochondria contains a binuclear iron center
inferred← citeshttps://doi.org/10.1016/0014-5793(95)00536-iopenalex-snapshot
Structural relationship between the mammalian Fe(III)‐Fe(II) and the Fe(III)‐Zn(II) plant purple acid phosphatases
inferred← citeshttps://doi.org/10.1016/0014-5793(95)00706-fopenalex-snapshot
Demonstration of segmental mobility in the functionally essential car☐yl terminal part of ribonucleotide reductase protein R2 from Escherichia coli
inferred← citeshttps://doi.org/10.1016/0014-5793(95)01067-oopenalex-snapshot
Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase
inferred← citeshttps://doi.org/10.1016/0014-5793(95)01082-popenalex-snapshot
Reduction of the tyrosyl radical and the iron center in protein R2 of ribonucleotide reductase from mouse, herpes simplex virus and E. coli by p‐alkoxyphenols
inferred← citeshttps://doi.org/10.1016/0014-5793(96)00480-2openalex-snapshot
The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals
inferred← citeshttps://doi.org/10.1016/0020-1693(94)04223-iopenalex-snapshot
An asymmetric homodinuclear complex containing the μ-oxo-bis(μ-carboxylato)diruthenium(III) core: X-ray structure of [Ru2O(O2CC6H4-p-OMe)3(en)(PPh3)2](ClO4)·3CHCl3
inferred← citeshttps://doi.org/10.1016/0020-1693(95)04803-0openalex-snapshot
Effect of substituents on the electrochemical behavior of basic iron acetates
inferred← citeshttps://doi.org/10.1016/0022-2364(91)90403-gopenalex-snapshot
Electron spin-lattice relaxation and spectral diffusion measurements on tyrosine radicals in proteins
inferred← citeshttps://doi.org/10.1016/0022-2836(92)90550-4openalex-snapshot
Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution
inferred← citeshttps://doi.org/10.1016/0022-2836(92)90913-5openalex-snapshot
Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath)
inferred← citeshttps://doi.org/10.1016/0022-2836(92)91012-eopenalex-snapshot
Crystallization and preliminary crystallographic data of purple acid phosphatase from red kidney bean
inferred← citeshttps://doi.org/10.1016/0042-6822(92)90907-7openalex-snapshot
Sequencing and 5′- and 3′-end transcript mapping of the gene encoding the small subunit of ribonucleotide reductase from bovine herpesvirus type-1
inferred← citeshttps://doi.org/10.1016/0076-6879(93)26028-8openalex-snapshot
[26] Detecting metal-metal interactions and measuring distances between metal centers in metalloproteins
inferred← citeshttps://doi.org/10.1016/0076-6879(94)43017-9openalex-snapshot
[15] Characterization of three proteins containing multiple iron sites: Rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster
inferred← citeshttps://doi.org/10.1016/0076-6879(95)58050-6openalex-snapshot
[18] X-ray crystallographic studies of cofactors in galactose oxidase
inferred← citeshttps://doi.org/10.1016/0147-0272(93)90012-qopenalex-snapshot
The clinical rationale for S-phase radiosensitization in human tumors
inferred← citeshttps://doi.org/10.1016/0167-4781(92)90151-oopenalex-snapshot
cDNA sequence of the small subunit of the hamster ribonucleotide reductase
inferred← citeshttps://doi.org/10.1016/0167-4781(94)90259-3openalex-snapshot
Large and small subunits of the Aujeszky's disease virus ribonucleotide reductase: Nucleotide sequence and putative structure
inferred← citeshttps://doi.org/10.1016/0167-4781(95)00168-9openalex-snapshot
Formation of a free radical of the sulfenylimine type in the mouse ribonucleotide reductase reaction with 2′-azido-2′-deoxycytidine 5′-diphosphate
inferred← citeshttps://doi.org/10.1016/0168-1702(93)90093-3openalex-snapshot
Analysis of the nucleotide sequence of a 43 kbp segment of the genome of variola virus India-1967 strain
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