Characterization of neutrophil b‐type cytochrome in situ by electron paramagnetic resonance spectroscopy

FEBS Letters

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