Dynamic regulation of the inducible nitric-oxide synthase by NO: comparison with the endothelial isoform.

@article{Gautier2004DynamicRO,
  title={Dynamic regulation of the inducible nitric-oxide synthase by NO: comparison with the endothelial isoform.},
  author={Cl{\'e}ment A. Gautier and Michel Negrerie and Z Q Wang and J. C. Lambry and Dennis J. Stuehr and Fabrice Collin and J Q Martin and Anny Slama-Schwok},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 6},
  pages={4358-65}
}
We studied by ultrafast time-resolved absorption spectroscopy the geminate recombination of NO to the oxygenase domain of the inducible NO synthase, iNOSoxy, and to mutated proteins at position Trp-457. This tryptophan interacts with the tetrahydrobiopterin cofactor BH4, and W457A/F mutations largely reduced the catalytic formation of NO. BH4 decreases the rate of NO rebinding to the ferric iNOSoxy compared with that measured in its absence. The pterin has a larger effect on W457A/F than on the… CONTINUE READING

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