Interactions of soluble guanylate cyclase with a P-site inhibitor: effects of gaseous heme ligands, azide, and allosteric activators on the binding of 2'-deoxy-3'-GMP.

@article{Makino2012InteractionsOS,
  title={Interactions of soluble guanylate cyclase with a P-site inhibitor: effects of gaseous heme ligands, azide, and allosteric activators on the binding of 2'-deoxy-3'-GMP.},
  author={Ryu Makino and Shinsuke Yazawa and Hiroshi Hori and Yoshitsugu Shiro},
  journal={Biochemistry},
  year={2012},
  volume={51 46},
  pages={
          9277-89
        }
}
Nitric oxide (NO) elicits a wide variety of physiological responses by binding to the heme in soluble guanylate cyclase (sGC) to stimulate cGMP production. Although nucleotides, such as ATP or GTP analogues, have been reported to regulate the signaling of NO binding from the heme site to the catalytic site, the other regulatory functions of nucleotides remain unexamined. Among the nucleotides tested, we found that 2'-d-3'-GMP acted as a potent noncompetitive inhibitor with respect to Mn-GTP… CONTINUE READING