Spectroscopic identification of the heme axial ligation of cytochrome b558 in the NADPH oxidase of porcine neutrophils.
Spectroscopic identification of the heme axial ligation of cytochrome b558 in the NADPH oxidase of porcine neutrophils.
复制标题
猪中性粒细胞 NADPH 氧化酶中细胞色素 b558 血红素轴向连接的光谱鉴定。
DOI：
10.1016/0014-5793(95)01372-5
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发表时间：
1995
期刊：
影响因子：
3.5
通讯作者：
Johnson,MK
中科院分区：
文献类型：
--
作者：
Fujii,H;Finnegan,MG;Miki,T;Crouse,BR;Kakinuma,K;Johnson,MK
应用低温电子顺磁共振（EPR）、近红外磁性圆二色性（NIR-MCD）和共振拉曼（RR）光谱，研究了猪血液中性粒细胞NADPH氧化酶低自旋细胞色素b558组分的轴向血红素连接。EPR和NIR-MCD结果表明，在冷冻溶液中存在两种不同的形式;一种在3.23处具有低场g值，卟啉（π）至Fe（III）的电荷转移最大值在1660 nm处，另一种在3.00处具有低场g值，卟啉（π）至Fe（III）的电荷转移最大值在1510 nm处。基于这些性质和RR研究，两者都归因于具有双组氨酸轴向连接的细胞色素b558的形式。所观察到的异质性的起源，位置和身份的特定组氨酸参与连接血红素，和血红素辅基的作用，在O2−生产的光，这些结果进行了讨论。
The combination of electron paramagnetic resonance (EPR), near-infrared magnetic circular dichroism (NIR-MCD) and resonance Raman (RR) spectroscopies at cryogenic temperatures has been used to identify the axial heme ligation of the low spin cytochrome b558component of NADPH oxidase from porcine blood neutrophils. The EPR and NIR-MCD results indicate the presence of two distinct forms in frozen solution; one with a low field g-value at 3.23 and porphyrin(π)-to-Fe(III) charge transfer maximum at 1660 nm and the other a low field g-value at 3.00 and porphyrin(π)-to-Fe(III) charge transfer maximum at 1510 nm. On the basis of these properties and the RR studies, both are attributed to forms of cytochrome b558with bis-histidine axial ligation. The origin of the observed heterogeneity, the location and identity of the specific histidines involved in ligating the heme, and the role of the heme prosthetic group in O2−production are discussed in light of these results.