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A Kinetic Analysis of the Activation of Soluble Guanylate Cyclase by Nitric Oxide

Author:
          Catherine Lloyd (Bioengineering Institute, University of Auckland)

Model Structure

In both pulmonary and vascular smooth muscle, nitric oxide (NO) acts as an activator of the enzyme soluble guanylate cyclase (sGC). sGC catalyses the conversion of guanosine 5'-triphosphate (GTP) to guanosine 3',5'-cyclic monophosphate (cGMP). Previous to this 2001 publication, (the complete original paper reference is cited below) binding rates of NO to sGC had only been measured in vitro under non-physiological conditions. Using their mathematical model (see Figure 1 below) and in vitro data, Condorelli and George provide a mechanism by which NO activates sGC in vivo.

In Vivo Control of Soluble Guanylate Cyclase Activation by Nitric Oxide: A Kinetic Analysis, Peter Condorelli and Steven C. George, 2001, Biophysical Journal, 80, 2110-2119. (A PDF version of the article is available for Journal Members on the Biophysical Journal website.) PubMed ID: 11325714

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diagram of the reaction pathway
Figure 1. A schematic diagram of the reactions involved in the binding of free nitric oxide (NO) to soluble guanylate cyclase (sGC). sGC catalyses the conversion of guanosine 5'-triphosphate (GTP) to guanosine 3',5'-cyclic monophosphate (cGMP).

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