Communication between the Zinc and Tetrahydrobiopterin Binding Sites in Nitric Oxide Synthase

@inproceedings{Chreifi2014CommunicationBT,
  title={Communication between the Zinc and Tetrahydrobiopterin
Binding Sites in Nitric Oxide
Synthase},
  author={Georges Chreifi and Huiying Li and Craig R. McInnes and Colin L. Gibson and Colin J. Suckling and Thomas L Poulos},
  booktitle={Biochemistry},
  year={2014}
}
The nitric oxide synthase (NOS) dimer is stabilized by a Zn(2+) ion coordinated to four symmetry-related Cys residues exactly along the dimer 2-fold axis. Each of the two essential tetrahydrobiopterin (H4B) molecules in the dimer interacts directly with the heme, and each H4B molecule is ~15 Å from the Zn(2+). We have determined the crystal structures of the bovine endothelial NOS dimer oxygenase domain bound to three different pterin analogues, which reveal an intimate structural communication… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 46 references

Nitric oxide synthases: Regulation and function

  • U. Forstermann, W. C. Sessa
  • Eur. Heart J. 33,
  • 2012

Formation of a protonated

  • K. K. Andersson
  • 2001