Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active [4Fe-4S](+) cluster of pyruvate formate-lyase activating enzyme.

@article{Walsby2002ElectronnuclearDR,
  title={Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active [4Fe-4S](+) cluster of pyruvate formate-lyase activating enzyme.},
  author={Charles J Walsby and Wei Hong and William E. Broderick and Jennifer Cheek and Danilo O. Ortillo and Joan B Broderick and Brian M Hoffman},
  journal={Journal of the American Chemical Society},
  year={2002},
  volume={124 12},
  pages={3143-51}
}
Pyruvate formate-lyase activating enzyme (PFL-AE) is a representative member of an emerging family of enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (AdoMet) to initiate radical catalysis. Although these enzymes have diverse functions, evidence is emerging that they operate by a common mechanism in which a [4Fe-4S](+) interacts with AdoMet to generate a 5'-deoxyadenosyl radical intermediate. To date, however, it has been unclear whether the iron-sulfur cluster is a simple… CONTINUE READING
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