{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["4(1)"],"submitter":["Petrova ON"],"pubmed_abstract":["Heme-Nitric oxide and Oxygen binding protein domains (H-NOX) are found in signaling pathways of both prokaryotes and eukaryotes and share sequence homology with soluble guanylate cyclase, the mammalian NO receptor. In bacteria, H-NOX is associated with kinase or methyl accepting chemotaxis domains. In the O<sub>2</sub>-sensor of the strict anaerobe Caldanaerobacter tengcongensis (Ct H-NOX) the heme appears highly distorted after O<sub>2</sub> binding, but the role of heme distortion in allosteric transitions was not yet evidenced. Here, we measure the dynamics of the heme distortion triggered by the dissociation of diatomics from Ct H-NOX using transient electronic absorption spectroscopy in the picosecond to millisecond time range. We obtained a spectroscopic signature of the heme flatten"],"journal":["Communications chemistry"],"pagination":["31"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9814294"],"repository":["biostudies-literature"],"pubmed_title":["Ultrafast dynamics of heme distortion in the O<sub>2</sub>-sensor of a thermophilic anaerobe bacterium."],"pmcid":["PMC9814294"],"pubmed_authors":["Negrerie M","Lamarre I","Selles J","Nioche P","Yoo BK","Petrova ON"],"additional_accession":[]},"is_claimable":false,"name":"Ultrafast dynamics of heme distortion in the O<sub>2</sub>-sensor of a thermophilic anaerobe bacterium.","description":"Heme-Nitric oxide and Oxygen binding protein domains (H-NOX) are found in signaling pathways of both prokaryotes and eukaryotes and share sequence homology with soluble guanylate cyclase, the mammalian NO receptor. In bacteria, H-NOX is associated with kinase or methyl accepting chemotaxis domains. In the O<sub>2</sub>-sensor of the strict anaerobe Caldanaerobacter tengcongensis (Ct H-NOX) the heme appears highly distorted after O<sub>2</sub> binding, but the role of heme distortion in allosteric transitions was not yet evidenced. Here, we measure the dynamics of the heme distortion triggered by the dissociation of diatomics from Ct H-NOX using transient electronic absorption spectroscopy in the picosecond to millisecond time range. We obtained a spectroscopic signature of the heme flatten","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2026-05-27T20:56:00.355Z","creation":"2024-12-03T17:18:28.186Z"},"accession":"S-EPMC9814294","cross_references":{"pubmed":["36697566"],"doi":["10.1038/s42004-021-00471-9"]}}