title: Characterization of neutrophil b-type cytochrome in situ by electron paramagnetic resonance spectroscopy.
abstract: Electron paramagnetic resonance spectroscopy at 4.2 K was successfully used to characterize neutrophil b-type cytochrome in situ. The spectra of resting neutrophils taken under aerobic conditions gave a set of characteristic signals in a high magnetic field (g = 2.85, 2.21 and 1.67) beside signals for myeloperoxidase and others. From the g values, shapes and the results of other experiments, these signals were attributed to those of cytochrome b558. The results indicate that cytochrome b558 in resting neutrophils is a hexa-coordinated ferric hemoprotein in a low-spin state. The obtained gz and gx values for the hemichrome were consistent with that of bis(imidazole)-coordinated hemoprotein.
authors.affiliation: Institute of Medical Science, University of Tokyo, Japan.
authors.forename: I
authors.initials: I
authors.lastname: Ueno
authors.forename: S
authors.initials: S
authors.lastname: Fujii
authors.forename: H
authors.initials: H
authors.lastname: Ohya-Nishiguchi
authors.forename: T
authors.initials: T
authors.lastname: Iizuka
authors.forename: S
authors.initials: S
authors.lastname: Kanegasaki
mesh_terms: D000818:Animals; D003573:Cytochrome b Group / Q000097:blood*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D019255:NADPH Oxidases; D009504:Neutrophils / Q000378:metabolism*; D013552:Swine
chemical_list: D003573:Cytochrome b Group; C036888:cytochrome b558; D019255:NADPH Oxidases