title: Degradation of human hemoglobin by organic C-nitroso compounds.
abstract: The crystal structure of the nitrosomethane adduct of human Hb shows N-binding of the MeNO ligands to heme Fe. The structure of the EtNO adduct reveals a surprising 4.9 Å heme slippage in the β subunit, and explains the ability of C-nitroso compounds to degrade Hb removing it from circulation.
authors.affiliation: Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, USA. yijun@ou.edu grichteraddo@ou.edu.
authors.forename: Jun
authors.initials: J
authors.lastname: Yi
authors.forename: Guan
authors.initials: G
authors.lastname: Ye
authors.forename: Leonard M
authors.initials: LM
authors.lastname: Thomas
authors.forename: George B
authors.initials: GB
authors.lastname: Richter-Addo
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006418:Heme / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D009603:Nitroso Compounds / Q000737:chemistry*; D020836:Protein Structure, Quaternary
chemical_list: D006454:Hemoglobins; D009603:Nitroso Compounds; D006418:Heme; C097158:nitrosomethane