{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jiang T"],"funding":["National Institute of Environmental Health Sciences","NIEHS NIH HHS","Division of Molecular and Cellular Biosciences","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["1395-1411"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11893013"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["63(11)"],"pubmed_abstract":["Nitric oxide synthase (NOS) in mammals is a family of multidomain proteins in which interdomain electron transfer (IET) is controlled by domain-domain interactions. Calmodulin (CaM) binds to the canonical CaM-binding site in the linker region between the FMN and heme domains of NOS and allows tethered FMN domain motions, enabling an intersubunit FMN-heme IET in the output state for NO production. Our previous cross-linking mass spectrometric (XL MS) results demonstrated site-specific protein dynamics in the CaM-responsive regions of rat neuronal NOS (nNOS) reductase construct, a monomeric protein [Jiang et al., <i>Biochemistry</i>, 2023, 62, 2232-2237]. In this work, we have extended our combined approach of XL MS structural mapping and AlphaFold structural prediction to examine the homodi"],"journal":["Biochemistry"],"pubmed_title":["Mapping the Intersubunit Interdomain FMN-Heme Interactions in Neuronal Nitric Oxide Synthase by Targeted Quantitative Cross-Linking Mass Spectrometry."],"pmcid":["PMC11893013"],"funding_grant_id":["2041692","P20GM130422","P30ES032755","P30 ES032755","P20 GM130422","R01 GM133973","GM133973"],"pubmed_authors":["Zhang H","Gyawali YP","Underbakke ES","Jiang T","Wan G","Feng C"],"additional_accession":[]},"is_claimable":false,"name":"Mapping the Intersubunit Interdomain FMN-Heme Interactions in Neuronal Nitric Oxide Synthase by Targeted Quantitative Cross-Linking Mass Spectrometry.","description":"Nitric oxide synthase (NOS) in mammals is a family of multidomain proteins in which interdomain electron transfer (IET) is controlled by domain-domain interactions. Calmodulin (CaM) binds to the canonical CaM-binding site in the linker region between the FMN and heme domains of NOS and allows tethered FMN domain motions, enabling an intersubunit FMN-heme IET in the output state for NO production. Our previous cross-linking mass spectrometric (XL MS) results demonstrated site-specific protein dynamics in the CaM-responsive regions of rat neuronal NOS (nNOS) reductase construct, a monomeric protein [Jiang et al., <i>Biochemistry</i>, 2023, 62, 2232-2237]. In this work, we have extended our combined approach of XL MS structural mapping and AlphaFold structural prediction to examine the homodi","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2025-04-22T11:10:01.625Z","creation":"2025-04-05T23:54:47.661Z"},"accession":"S-EPMC11893013","cross_references":{"pubmed":["38747545"],"doi":["10.1021/acs.biochem.4c00157"]}}