Kinetics of Radical Intermediate Formation and Deoxynucleotide Production in 3-Aminotyrosine-Substituted Escherichia coli Ribonucleotide Reductases - sprookjes - yvandenbroek - TriplyDB

Kinetics of Radical Intermediate Formation and Deoxynucleotide Production in 3-Aminotyrosine-Substituted Escherichia coli Ribonucleotide Reductases

Kinetics of Radical Intermediate Formation and Deoxynucleotide Production in 3-Aminotyrosine-Substituted Escherichia coli Ribonucleotide Reductases

http://www.wikidata.org/entity/Q27667992

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Moving protons and electrons in biomimetic systems At the Interface of Chemical and Biological Synthesis: An Expanded Genetic Code.Deciphering radical transport in the large subunit of class I ribonucleotide reductase Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli.Generation of a stable, aminotyrosyl radical-induced α2β2 complex of Escherichia coli class Ia ribonucleotide reductase.Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example Photochemical Generation of a Tryptophan Radical within the Subunit Interface of Ribonucleotide Reductase.Radical-translocation intermediates and hurdling of pathway defects in "super-oxidized" (Mn(IV)/Fe(IV)) Chlamydia trachomatis ribonucleotide reductase.Biochemical analysis with the expanded genetic lexicon.The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years.Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.Equilibration of tyrosyl radicals (Y356•, Y731•, Y730•) in the radical propagation pathway of the Escherichia coli class Ia ribonucleotide reductase.Reverse Electron Transfer Completes the Catalytic Cycle in a 2,3,5-Trifluorotyrosine-Substituted Ribonucleotide Reductase.A >200 meV Uphill Thermodynamic Landscape for Radical Transport in Escherichia coli Ribonucleotide Reductase Determined Using Fluorotyrosine-Substituted Enzymes.Modulation of Y356 photooxidation in E. coli class Ia ribonucleotide reductase by Y731 across the α2:β2 interface.Kinetics of hydrogen atom abstraction from substrate by an active site thiyl radical in ribonucleotide reductase Electron hopping through proteins.Proton Coupled Electron Transfer and Redox Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II.ENDOR spectroscopy and DFT calculations: evidence for the hydrogen-bond network within α2 in the PCET of E. coli ribonucleotide reductase.Charge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase.Hydrogen bond network between amino acid radical intermediates on the proton-coupled electron transfer pathway of E. coli α2 ribonucleotide reductase.Redox-linked conformational control of proton-coupled electron transfer: Y122 in the ribonucleotide reductase β2 subunit.Reversible, long-range radical transfer in E. coli class Ia ribonucleotide reductase.Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase.Expanding and reprogramming the genetic code.Playing with the molecules of life.Glutamate 52-β at the α/β subunit interface of Escherichia coli class Ia ribonucleotide reductase is essential for conformational gating of radical transfer.Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm.Disruption of an oligomeric interface prevents allosteric inhibition of Escherichia coli class Ia ribonucleotide reductase.Radical transfer in E. coli ribonucleotide reductase: a NH2Y731/R411A-α mutant unmasks a new conformation of the pathway residue 731.Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase Biosynthetic approach to modeling and understanding metalloproteins using unnatural amino acids

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Kinetics of Radical Intermediate Formation and Deoxynucleotide Production in 3-Aminotyrosine-Substituted Escherichia coli Ribonucleotide Reductases

http://www.wikidata.org/entity/Q27667992

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2011 nî lūn-bûn

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2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2011 թվականի հունիսին հրատարակված գիտական հոդված

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2011年の論文

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

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Journal of the American Chemical Society

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Kinetics of Radical Intermedia ...... coli Ribonucleotide Reductases

@en

P2093

Ellen C Minnihan

http://www.w3.org/2001/XMLSchema#string

Mohammad R Seyedsayamdost

http://www.w3.org/2001/XMLSchema#string

Ulla Uhlin

http://www.w3.org/2001/XMLSchema#string

P2860

Three-dimensional structure of the free radical protein of ribonucleotide reductase

Improved methods for building protein models in electron density maps and the location of errors in these models

Site-Specific Incorporation of 3-Nitrotyrosine as a Probe of p K a Perturbation of Redox-Active Tyrosines in Ribonucleotide Reductase

A Hot Oxidant, 3-NO 2 Y 122 Radical, Unmasks Conformational Gating in Ribonucleotide Reductase

Structure of ribonucleotide reductase protein R1

The CCP4 suite: programs for protein crystallography

Ribonucleotide reductases

De novo proteins as models of radical enzymes.

Ribonucleotide reductases.

Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B.

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9430-40

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scholarly article

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953825

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10.1021/JA201640N

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24

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133

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21612216

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3125130

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