Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2.

@article{Matthews2009SubstratetriggeredFA,
  title={Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2.},
  author={Megan L Matthews and Courtney M. Krest and Eric W. Barr and Fr{\'e}d{\'e}ric H. Vaillancourt and Christopher T Walsh and Michael T. Green and Carsten Krebs and J Martin Bollinger},
  journal={Biochemistry},
  year={2009},
  volume={48 20},
  pages={4331-43}
}
Aliphatic halogenases activate O(2), cleave alpha-ketoglutarate (alphaKG) to CO(2) and succinate, and form haloferryl [X-Fe(IV)O; X = Cl or Br] complexes that cleave aliphatic C-H bonds to install halogens during the biosynthesis of natural products by non-ribosomal peptide synthetases (NRPSs). For the related alphaKG-dependent dioxygenases, it has been shown that reaction of the Fe(II) cofactor with O(2) to form the C-H bond-cleaving ferryl complex is "triggered" by binding of the target… CONTINUE READING

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Luo, Y.-R
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