Structure of cinaciguat (BAY 58-2667) bound to Nostoc H-NOX domain reveals insights into heme-mimetic activation of the soluble guanylyl cyclase.

@article{Martin2010StructureOC,
  title={Structure of cinaciguat (BAY 58-2667) bound to Nostoc H-NOX domain reveals insights into heme-mimetic activation of the soluble guanylyl cyclase.},
  author={Faye E Martin and Padmamalini Baskaran and Xiaolei Ma and Pete W. Dunten and Martina Schaefer and J. -P. Stasch and Annie V. Beuve and Focco van den Akker},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 29},
  pages={22651-7}
}
Heme is a vital molecule for all life forms with heme being capable of assisting in catalysis, binding ligands, and undergoing redox changes. Heme-related dysfunction can lead to cardiovascular diseases with the oxidation of the heme of soluble guanylyl cyclase (sGC) critically implicated in some of these cardiovascular diseases. sGC, the main nitric oxide (NO) receptor, stimulates second messenger cGMP production, whereas reactive oxygen species are known to scavenge NO and oxidize/inactivate… CONTINUE READING