Designed metalloprotein stabilizes a semiquinone radical.

@article{Ulas2016DesignedMS,
  title={Designed metalloprotein stabilizes a semiquinone radical.},
  author={G{\"o}zde Ulas and Thomas M. Lemmin and Yibing Wu and George Gassner and William F. DeGrado},
  journal={Nature chemistry},
  year={2016},
  volume={8 4},
  pages={354-9}
}
Enzymes use binding energy to stabilize their substrates in high-energy states that are otherwise inaccessible at ambient temperature. Here we show that a de novo designed Zn(II) metalloprotein stabilizes a chemically reactive organic radical that is otherwise unstable in aqueous media. The protein binds tightly to and stabilizes the radical semiquinone form of 3,5-di-tert-butylcatechol. Solution NMR spectroscopy in conjunction with molecular dynamics simulations show that the substrate binds… CONTINUE READING
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