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3,5-difluorotyrosine

Known as: Tyrosine, 3,5-difluoro, difluorotyrosine 
 
National Institutes of Health

Related topics

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2 relations

Broader (1)

Tyrosine
analogs & derivatives

Papers overview

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2017
2017
Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.
Redox-active tyrosines (Ys) play essential roles in enzymes involved in primary metabolism including energy transduction and… Expand
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2017
2017
Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.
Escherichia coli class Ia ribonucleotide reductase (RNR) is composed of two subunits that form an active α2β2 complex. The… Expand
2016
2016
A >200 meV Uphill Thermodynamic Landscape for Radical Transport in Escherichia coli Ribonucleotide Reductase Determined Using Fluorotyrosine-Substituted Enzymes
Escherichia coli class Ia ribonucleotide reductase (RNR) converts ribonucleotides to deoxynucleotides. A diferric-tyrosyl radical… Expand
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2015
2015
Fluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane Insertion*
Background: Peripheral membrane proteins can interact with zwitterionic phospholipid headgroups or lipid tails. Results… Expand
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2014
2014
Nano-size uni-lamellar lipodisq improved in situ auto-phosphorylation analysis of E. coli tyrosine kinase using 19F nuclear magnetic resonance
Among many of biophysical methods, F NMR spectroscopy has emerged as a powerful tool for characterizing protein structure… Expand
2013
2013
Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.
The reversible Y-O•/Y-OH redox properties of the α3Y model protein allow access to the electrochemical and thermodynamic… Expand
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2013
2013
A genetically encoded 19F NMR probe for tyrosine phosphorylation.
Tyrosine phosphorylation is a pivotal post-translational modification (PTM) which regulates enzymatic activity, protein… Expand
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2013
2013
Modulation of Y [subscript 356] Photooxidation in E. Coli Class Ia Ribonucleotide Reductase by Y [subscript 731] Across the α [subscript 2] :β [subscript 2] Interface
Substrate turnover in class Ia ribonucleotide reductase (RNR) requires reversible radical transport across two subunits over 35 A… Expand
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2008
2008
Synthesis of 3,5-difluorotyrosine-containing peptides: application in substrate profiling of protein tyrosine phosphatases.
Fully protected 3,5-difluorotyrosine (F2Y), Fmoc-F2Y(tBu)-OH, is efficiently prepared by a chemoenzymatic process and… Expand
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2003
2003
The role of acidic dissociation of substrate's phenol group in the mechanism of tyrosine phenol-lyase.
pH dependencies of the main kinetic parameters for the reaction of tyrosine phenol-lyase (TPL) with L-tyrosine were studied… Expand
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