Ueno I, Fujii S, Ohya-Nishiguchi H, Iizuka T, Kanegasaki S
Institute of Medical Science, University of Tokyo, Japan.
FEBS Lett. 1991 Apr 9;281(1-2):130-2. doi: 10.1016/0014-5793(91)80375-d.
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.
4.2K下的电子顺磁共振光谱被成功用于原位表征中性粒细胞b型细胞色素。在有氧条件下采集的静息中性粒细胞光谱，除了髓过氧化物酶和其他物质的信号外，在高磁场中还给出了一组特征信号（g = 2.85、2.21和1.67）。根据g值、形状和其他实验结果，这些信号归因于细胞色素b558的信号。结果表明，静息中性粒细胞中的细胞色素b558是一种处于低自旋状态的六配位铁血红蛋白。所获得的半高铁血红素的gz和gx值与双（咪唑）配位血红蛋白的值一致。
