The ferredoxin-like domain of the activating enzyme is required for generating a lasting glycyl radical in 4-hydroxyphenylacetate decarboxylase

@article{Selvaraj2014TheFD,
  title={The ferredoxin-like domain of the activating enzyme is required for generating a lasting glycyl radical in 4-hydroxyphenylacetate decarboxylase},
  author={Brinda Selvaraj and Antonio J. Pierik and Eckhard Bill and Berta Maria Martins},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2014},
  volume={19},
  pages={1317-1326}
}
4-Hydroxyphenylacetate decarboxylase-activating enzyme (4Hpad-AE) uses S-adenosylmethionine (SAM or AdoMet) and a [4Fe-4S]2+/+ cluster (RS cluster) to generate a stable glycyl radical on the decarboxylase. 4Hpad-AE might bind up to two auxiliary [4Fe-4S] clusters coordinated by a ferredoxin-like insert C-terminal to the RS cluster-binding motif. Except for… CONTINUE READING