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Background Nitric oxide binds with the heme moiety of sGC and activates sGC several hundred folds the cGMP-forming activity of the enzyme. Although nitric oxide is the major physiological regulator of sGC function, the extent of this activation is influenced by a number of cellular factors, e.g. ATP, substrate GTP, reaction products, intracellular calcium, etc. Several proteins, such as HSP70, HSP90 and CCTh, where shown to interact with sGC and modulate its function.

G-protein regulator LGN inhibits the activity of soluble guanylyl cyclase