ArticleBiochemistry2025
Oxidative Activation of the Heme Nitric Oxide/Oxygen-Binding Protein (H-NOX) from
Article in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The heme nitric oxide/oxygen-binding proteins (H-NOX) are bacterial homologues of the sensor domain of mammalian soluble guanylate cyclase (sGC), a multidomain enzyme that catalyzes the production of cyclic guanosine monophosphate (cGMP) in response to NO. In facultative anaerobes, H-NOX proteins sense nitric oxide (NO) and regulate various communal behaviors including biofilm formation, motility, virulence, and quorum sensing. Rupture of the proximal heme iron-histidine bond during the formation of a five-coordinate low-spin ferrous nitrosyl (5cLS Fe(II)-NO) heme is thought to be required for H-NOX activation, allowing them to interact with downstream signaling partners such as diguanylate cyclases (DGC), phosphodiesterases (PDE), or histidine kinases (HK). Some H-NOX homologues also contain a conserved Cys-ligated zinc-binding site, which can respond to oxidative stress, at least
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