Crystal structure of HydF scaffold protein provides insights into [FeFe]-hydrogenase maturation.

  title={Crystal structure of HydF scaffold protein provides insights into [FeFe]-hydrogenase maturation.},
  author={Laura Cendron and Paola Berto and Sarah D'Adamo and Francesca Vallese and Chiara Govoni and Matthew C. Posewitz and Giorgio Mario Giacometti and Paola Costantini and Giuseppe Zanotti},
  journal={The Journal of biological chemistry},
  volume={286 51},
[FeFe]-hydrogenases catalyze the reversible production of H2 in some bacteria and unicellular eukaryotes. These enzymes require ancillary proteins to assemble the unique active site H-cluster, a complex structure composed of a 2Fe center bridged to a [4Fe-4S] cubane. The first crystal structure of a key factor in the maturation process, HydF, has been determined at 3 Å resolution. The protein monomer present in the asymmetric unit of the crystal comprises three domains: a GTP-binding domain, a… CONTINUE READING

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