NO binds to the distal site of haem in the fully activated soluble guanylate cyclase

Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO). The binding of NO to the haem of sGC induces a large conformational change in the enzyme and activates its cyclase activity. However, whether NO binds to the proximal site or the distal site of haem in the fully activated state remains under debate. Here, we present cryo-EM maps of sGC in the NO-activated state at high resolutions, allowing the observation of the density of NO. These cryo-EM maps show the binding of NO to the distal site of haem in the NO-activated state.

Automated summary

Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO) and its binding to the distal site of haem in the fully activated state has been observed through high-resolution cryo-EM maps. The binding of NO induces a conformational change in sGC and activates its cyclase activity.