Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: structure studies of a cysteine thiolate-liganded heme protein that hydroxylates L-arginine to produce NO. as a cellular signal.

@article{Masters1996NeuronalNO,
  title={Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: structure studies of a cysteine thiolate-liganded heme protein that hydroxylates L-arginine to produce NO. as a cellular signal.},
  author={Bettie Sue Siler Masters and Kirk McMillan and E A Sheta and Jonathan S. Nishimura and Linda J. Roman and P Martasek},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={1996},
  volume={10 5},
  pages={552-8}
}
The nitric oxide synthases (NOS-I, neuronal, NOS-II, inducible, and NOS-III, endothelial) are the most recent additions to the large number of heme proteins that contain cysteine thiolate-liganded protoporphyrin IX heme prosthetic groups. This group of oxygenating enzymes also includes one of the largest gene families, that of the cytochromes P450, which have been demonstrated to be involved in the hydroxylation of a variety of substrates, including endogenous compounds (steroids, fatty acids… CONTINUE READING