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 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.

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