The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase. Epr and electron nuclear double resonance studies on a new transient tryptophan radical.

@article{Poetsch1999TheIR,
  title={The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase. Epr and electron nuclear double resonance studies on a new transient tryptophan radical.},
  author={Stephan Poetsch and Friedhelm Lendzian and Rolf Ingemarson and Andreas H{\"o}rnberg and Lars Thelander and Wolfgang Lubitz and G{\"u}nter Lassmann and Astrid Gr{\"a}slund},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 25},
  pages={17696-704}
}
The ferrous iron/oxygen reconstitution reaction in protein R2 of mouse and Escherichia coli ribonucleotide reductase (RNR) leads to the formation of a stable protein-linked tyrosyl radical and a mu-oxo-bridged diferric iron center, both necessary for enzyme activity. We have studied the reconstitution reaction in three protein R2 mutants Y177W, Y177F, and Y177C of mouse RNR to investigate if other residues at the site of the radical forming Tyr-177 can harbor free radicals. In Y177W we observed… CONTINUE READING

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