Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.

@article{Minnihan2011IncorporationOF,
  title={Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.},
  author={E. Minnihan and D. Young and P. Schultz and J. Stubbe},
  journal={Journal of the American Chemical Society},
  year={2011},
  volume={133 40},
  pages={
          15942-5
        }
}
Tyrosyl radicals (Y·s) are prevalent in biological catalysis and are formed under physiological conditions by the coupled loss of both a proton and an electron. Fluorotyrosines (F(n)Ys, n = 1-4) are promising tools for studying the mechanism of Y· formation and reactivity, as their pK(a) values and peak potentials span four units and 300 mV, respectively, between pH 6 and 10. In this manuscript, we present the directed evolution of aminoacyl-tRNA synthetases (aaRSs) for 2,3,5-trifluorotyrosine… Expand
Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase.
Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.
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