Oxidative Activation of the Heme Nitric Oxide/Oxygen-Binding Protein (H-NOX) from <i>Caulobacter crescentus</i>.

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 cont

SUBMITTER: Alatishe A 

PROVIDER: S-EPMC12329717 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature