title: (1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state.
abstract: The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 is a monomeric 123-residue Group I 2/2 hemoglobin. Here, we report (1)H, (15)N, and (13)C assignments for the ferric (low-spin, S = (1/2)) protein with a b heme cofactor and after post-translational modification leading to a c-like heme.
authors.affiliation: T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Pond
authors.forename: David A
authors.initials: DA
authors.lastname: Vuletich
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Falzone
authors.forename: Ananya
authors.initials: A
authors.lastname: Majumdar
authors.forename: Juliette T J
authors.initials: JT
authors.lastname: Lecomte
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D006639:Histidine; D007501:Iron; D019906:Nuclear Magnetic Resonance, Biomolecular; D011499:Protein Processing, Post-Translational; D046940:Synechococcus
chemical_list: D001426:Bacterial Proteins; D006454:Hemoglobins; D006418:Heme; D006639:Histidine; D007501:Iron