Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase.

@article{Tejero2008StabilizationAC,
  title={Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase.},
  author={Jes{\'u}s Tejero and Ashis Biswas and Zhi-qiang Wang and Richard C Page and Mohammad Mahfuzul Haque and Craig F Hemann and Jay L. Zweier and Saurav Misra and Dennis J Stuehr},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 48},
  pages={
          33498-507
        }
}
Nitric-oxide synthases (NOS) are heme-thiolate enzymes that N-hydroxylate L-arginine (L-Arg) to make NO. NOS contain a unique Trp residue whose side chain stacks with the heme and hydrogen bonds with the heme thiolate. To understand its importance we substituted His for Trp188 in the inducible NOS oxygenase domain (iNOSoxy) and characterized enzyme spectral, thermodynamic, structural, kinetic, and catalytic properties. The W188H mutation had relatively small effects on l-Arg binding and on… CONTINUE READING

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