On the activation of soluble guanylyl cyclase by nitric oxide.

ABSTRACT: Soluble guanylyl cyclase (sGC) is the major cellular receptor for the intercellular messenger nitric oxide (NO) and mediates a wide range of physiological effects through elevation of intracellular cGMP levels. Critical to our understanding of how NO signals are decoded by receptive cells and translated into a useful physiological response is an appreciation of the molecular and kinetic details of the mechanism by which NO activates sGC. It is known that NO binds to a haem prosthetic group on the receptor and triggers a conformational change that increases the catalysis of cGMP synthesis by several hundred-fold. The haem is covalently attached to sGC at His-105 of the beta1 subunit, and it was thought previously that activation of sGC by NO occurs in two steps: binding of NO to the haem to

SUBMITTER: Bellamy TC 

PROVIDER: S-EPMC117590 | biostudies-literature | 2002 Jan

REPOSITORIES: biostudies-literature