FEBS Letters | |
Characterization of neutrophil b‐type cytochrome in situ by electron paramagnetic resonance spectroscopy | |
Fujii, Satoshi2  Ohya-Nishiguchi, Hiroaki2  Kanegasaki, Shiro3  Ueno, Ikuko3  Iizuka, Tetsutaro1  | |
[1] The Institute of Physical and Chemical Research, Wako-shi, Saitama 351-01, Japan;Department of Chemistry, Faculty of Science, Kyoto University, Sakyoku, Kyoto 606, Japan;The Institute of Medical Science, The University of Tokyo, Minatoku, Tokyo 108, Japan | |
关键词: Cytochrome b558; Neutrophil; EPR spectroscopy; O 2 −generation; Crystal field splitting parameter; EPR; electron paramagnetic resonance; O2; superoxide anion; MPO; myeloperoxidase; SOD; superoxide dismutase; | |
DOI : 10.1016/0014-5793(91)80375-D | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Electron paramagnetic resonance spectroscopy at 4.2 K was successfully used to characterize neutrophil b-type cytochrome in situ. The spectra or 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 b 558. The results indicate that cytochrome b 558 in resting neutrophils is a hexa-coordinated ferric hemoprotein in a low-spin state. The obtained g??? and g??? values for the hemichrome were consistent with that of bis(imiduzole)-coordinated hemoprotein.
【 授权许可】
Unknown
【 预 览 】
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RO201912020294680ZK.pdf | 424KB | download |