The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.

ABSTRACT: Some classes of bacteria within phyla possess protein sensors identified as homologous to the heme domain of soluble guanylate cyclase, the mammalian NO-receptor. Named H-NOX domain (Heme-Nitric Oxide or OXygen-binding), their heme binds nitric oxide (NO) and O₂ for some of them. The signaling pathways where these proteins act as NO or O₂ sensors appear various and are fully established for only some species. Here, we investigated the reactivity of H-NOX from bacterial species toward NO with a mechanistic point of view using time-resolved spectroscopy. The present data show that H-NOXs modulate the dynamics of NO as a function of temperature, but in different ranges, changing its affinity by changing the probability of NO rebinding after dissociation in the picosecond

SUBMITTER: Yoo BK 

PROVIDER: S-EPMC10411614 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature