Revisiting the kinetics of nitric oxide (NO) binding to soluble guanylate cyclase: the simple NO-binding model is incorrect.

@article{Ballou2002RevisitingTK,
  title={Revisiting the kinetics of nitric oxide (NO) binding to soluble guanylate cyclase: the simple NO-binding model is incorrect.},
  author={David P. Ballou and Yunde Zhao and Philip E Brandish and Michael A Marletta},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 19},
  pages={12097-101}
}
Soluble guanylate cyclase (sGC) is a ferrous iron hemoprotein receptor for nitric oxide (NO). NO binding to the heme activates the enzyme 300-fold. sGC as isolated is five-coordinate, ferrous with histidine as the axial ligand. The NO-activated enzyme is a five-coordinate nitrosyl complex where the axial histidine bond is broken. Past studies using rapid-reaction kinetics demonstrated that both the formation of a six-coordinate intermediate and the conversion of the intermediate to the… CONTINUE READING