title: Analyzing heme proteins using EPR techniques: the heme-pocket structure of ferric mouse neuroglobin.
abstract: In this work, an electron paramagnetic resonance (EPR) strategy to study the heme-pocket structure of low-spin ferric heme proteins is optimized. Frozen solutions of ferric mouse neuroglobin (mNgb) are analyzed by means of electron spin echo envelope modulation and pulsed electron-nuclear double resonance techniques. The hyperfine and nuclear quadrupole couplings of the directly coordinating heme and histidine nitrogens are derived and are discussed in comparison with known data of other ferric porphyrin compounds. In combination with the hyperfine matrices of the imidazole protons, the 14N EPR parameters reveal structural information on the heme pocket of mNgb that is in agreement with previous X-ray diffraction data on neuroglobins.
authors.affiliation: Department of Physics, University of Antwerp, Campus Drie Eiken, Universiteitsplein 1, 2610 Wilrijk, Belgium.
authors.forename: E
authors.initials: E
authors.lastname: Vinck
authors.forename: S
authors.initials: S
authors.lastname: Van Doorslaer
authors.forename: S
authors.initials: S
authors.lastname: Dewilde
authors.forename: G
authors.initials: G
authors.lastname: Mitrikas
authors.forename: A
authors.initials: A
authors.lastname: Schweiger
authors.forename: L
authors.initials: L
authors.lastname: Moens
mesh_terms: D000818:Animals; D003198:Computer Simulation; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D005290:Ferric Compounds / Q000737:chemistry* / Q000378:metabolism; D005914:Globins / Q000737:chemistry* / Q000378:metabolism; D006420:Hemeproteins / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008956:Models, Chemical; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D000078787:Neuroglobin
chemical_list: D005290:Ferric Compounds; D006420:Hemeproteins; D009419:Nerve Tissue Proteins; D000078787:Neuroglobin; D005914:Globins