{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jayaraman T"],"funding":["NHLBI NIH HHS"],"pagination":["42679-42689"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3234913"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["286(49)"],"pubmed_abstract":["Neuroglobin protects neurons from hypoxia in vitro and in vivo; however, the underlying mechanisms for this effect remain poorly understood. Most of the neuroglobin is present in a hexacoordinate state with proximal and distal histidines in the heme pocket directly bound to the heme iron. At equilibrium, the concentration of the five-coordinate neuroglobin remains very low (0.1-5%). Recent studies have shown that post-translational redox regulation of neuroglobin surface thiol disulfide formation increases the open probability of the heme pocket and allows nitrite binding and reaction to form NO. We hypothesized that the equilibrium between the six- and five-coordinate states and secondary reactions with nitrite to form NO could be regulated by other hypoxia-dependent post-translational mo"],"journal":["The Journal of biological chemistry"],"pubmed_title":["14-3-3 binding and phosphorylation of neuroglobin during hypoxia modulate six-to-five heme pocket coordination and rate of nitrite reduction to nitric oxide."],"pmcid":["PMC3234913"],"funding_grant_id":["R01 HL096973","R01 HL095973","R01 HL098032","R01 HL098174","P01 HL103455","R01 HL097376","R01 HL096376"],"pubmed_authors":["Blood AB","Shapiro C","Frizzell S","Chen BB","Tiso M","Mallampalli RK","Tejero J","Zhao X","Jayaraman T","Conrads TP","Hood BL","Gladwin MT","Wang X"],"additional_accession":[]},"is_claimable":false,"name":"14-3-3 binding and phosphorylation of neuroglobin during hypoxia modulate six-to-five heme pocket coordination and rate of nitrite reduction to nitric oxide.","description":"Neuroglobin protects neurons from hypoxia in vitro and in vivo; however, the underlying mechanisms for this effect remain poorly understood. Most of the neuroglobin is present in a hexacoordinate state with proximal and distal histidines in the heme pocket directly bound to the heme iron. At equilibrium, the concentration of the five-coordinate neuroglobin remains very low (0.1-5%). Recent studies have shown that post-translational redox regulation of neuroglobin surface thiol disulfide formation increases the open probability of the heme pocket and allows nitrite binding and reaction to form NO. We hypothesized that the equilibrium between the six- and five-coordinate states and secondary reactions with nitrite to form NO could be regulated by other hypoxia-dependent post-translational mo","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Dec","modification":"2025-04-26T20:45:54.911Z","creation":"2019-06-05T16:56:16Z"},"accession":"S-EPMC3234913","cross_references":{"pubmed":["21965683"],"doi":["10.1074/jbc.M111.271973","10.1074/jbc.m111.271973"]}}