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Background Soluble guanylate cyclase (sGC) is the main receptor of nitric oxide (NO). NO binds to the ferrous heme moiety of sGC thus activating the enzyme and increasing cyclic GMP (cGMP) levels. sGC is inhibited by various oxidants which either convert ferrous heme to ferric suppressing NO binding or modify essential thiol groups of sGC. Certain heat shock proteins (Hsp) can protect the enzymes from this inactivation. Hence, we suggested that Hsp can block oxidant-induced inhibition of sGC.

Regulation of soluble guanylate cyclase activity by direct interaction with heat shock protein Hsp90