Inducible nitric oxide synthase: role of the N-terminal beta-hairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction.

@article{Ghosh1999InducibleNO,
  title={Inducible nitric oxide synthase: role of the N-terminal beta-hairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction.},
  author={Dipak K. Ghosh and Brian R Crane and Sanjay Ghosh and Dennis W Wolan and Ratan Gachhui and Casey Crooks and Anthony Presta and John A. Tainer and Elizabeth D. Getzoff and Dennis J. Stuehr},
  journal={The EMBO journal},
  year={1999},
  volume={18 22},
  pages={6260-70}
}
The oxygenase domain of the inducible nitric oxide synthase (iNOSox; residues 1-498) is a dimer that binds heme, L-arginine and tetrahydrobiopterin (H(4)B) and is the site for nitric oxide synthesis. We examined an N-terminal segment that contains a beta-hairpin hook, a zinc ligation center and part of the H(4)B-binding site for its role in dimerization, catalysis, and H(4)B and substrate interactions. Deletion mutagenesis identified the minimum catalytic core and indicated that an intact N… CONTINUE READING
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