The HydG Enzyme Generates an Fe(CO)2(CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster

@article{Kuchenreuther2014TheHE,
  title={The HydG Enzyme Generates an Fe(CO)2(CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster},
  author={Jon M. Kuchenreuther and William K Myers and Daniel L M Suess and Troy A Stich and Vladimir Pelmenschikov and Stacey A. Shiigi and Stephen P Cramer and James R. Swartz and R David Britt and Simon J. George},
  journal={Science},
  year={2014},
  volume={343},
  pages={424-427}
}
Three iron-sulfur proteins–HydE, HydF, and HydG–play a key role in the synthesis of the [2Fe]H component of the catalytic H-cluster of FeFe hydrogenase. The radical S-adenosyl-l-methionine enzyme HydG lyses free tyrosine to produce p-cresol and the CO and CN− ligands of the [2Fe]H cluster. Here, we applied stopped-flow Fourier transform infrared and electron-nuclear double resonance spectroscopies to probe the formation of HydG-bound Fe-containing species bearing CO and CN− ligands with… CONTINUE READING
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