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Soluble guanylate cyclase (sGC), a heme containing α/βheterodimer, is one of the crucial enzymes within the NO/ cGMP signaling pathway. The enzyme becomes activated up to 200-fold upon binding of its physiological activator nitric oxide (NO) to the prosthetic heme moiety. sGC activation by NO requires the presence of the reduced Fe2+ heme moiety and oxidation to its ferric Fe3+ state abolishes any NO-induced enzyme activation. Based on this observation specific sGC inhibitors such as ODQ were developed which show a higher specificity for the sGC heme than general heme oxidants such as methyleneblue or ferricyanide.

Formation of quasi-covalent sGC α1/β1-heterodimers by ODQ-induced oxidation of the prosthetic heme moiety