Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer.

@article{Klatt1995StructuralAO,
  title={Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer.},
  author={Peter Klatt and Kurt Schmidt and Dietrich Lehner and Otto Glatter and Hans Peter B{\"a}chinger and B Mayer},
  journal={The EMBO journal},
  year={1995},
  volume={14 15},
  pages={3687-95}
}
Nitric oxide synthases (NOSs), which catalyze the formation of the ubiquitous biological messenger molecule nitric oxide, represent unique cytochrome P-450s, containing reductase and mono-oxygenase domains within one polypeptide and requiring tetrahydrobiopterin as cofactor. To investigate whether tetrahydrobiopterin functions as an allosteric effector of NOS, we have analyzed the effect of the pteridine on the conformation of neuronal NOS purified from porcine brain by means of circular… CONTINUE READING

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