Characterization of neutrophil b-type cytochrome in situ by electron paramagnetic resonance spectroscopy.
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.
Ueno
I
I
Institute of Medical Science, University of Tokyo, Japan.
Fujii
S
S
Ohya-Nishiguchi
H
H
Iizuka
T
T
Kanegasaki
S
S
D000818:Animals; D003573:Cytochrome b Group / Q000097:blood*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D019255:NADPH Oxidases; D009504:Neutrophils / Q000378:metabolism*; D013552:Swine
D003573:Cytochrome b Group; C036888:cytochrome b558; D019255:NADPH Oxidases