Koshkin V, Pick E
Department of Human Microbiology, Sackler School of Medicine, Tel-Aviv University, Israel.
FEBS Lett. 1993 Jul 19;327(1):57-62. doi: 10.1016/0014-5793(93)81039-3.
Purified cytochrome b559 from guinea pig macrophages was relipidated with several phospholipid mixtures. Relipidated cytochrome b559 was found capable of NADPH-dependent superoxide (O2-) production in the absence of the cytosolic components of the NADPH oxidase complex. The rate of O2- generation by cytochrome b559 varied with the type of phospholipid utilized for relipidation, was absolutely dependent on exogenous FAD, and was enhanced by a critical concentration of anionic amphiphile. It is demonstrated that exogenous FAD acts by binding to cytochrome b559. These results provide firm experimental evidence for the proposal that cytochrome b559 comprises the complete electron transporting apparatus of the O2- forming NADPH oxidase and that the cytosolic components function merely as activators.
用几种磷脂混合物对从豚鼠巨噬细胞中纯化得到的细胞色素b559进行了再脂化处理。结果发现，再脂化的细胞色素b559在没有NADPH氧化酶复合体胞质成分的情况下，能够产生依赖NADPH的超氧化物（O2-）。细胞色素b559产生O2-的速率随用于再脂化的磷脂类型而变化，绝对依赖于外源性FAD，并被临界浓度的阴离子两亲物增强。结果表明，外源性FAD通过与细胞色素b559结合起作用。这些结果为以下提议提供了确凿的实验证据：细胞色素b559构成了形成O2-的NADPH氧化酶的完整电子传输装置，而胞质成分仅起激活剂的作用。
