Mauk M R, Reid L S, Mauk A G
Biochem J. 1984 Jul 15;221(2):297-302. doi: 10.1042/bj2210297.
Ferricytochrome b5 was found to convert oxyhaemoglobin into methaemoglobin under conditions previously found to be optimal for complex-formation between ferricytochrome b5 and methaemoglobin [Mauk & Mauk (1982) Biochemistry 21, 4730-4734]. As this reaction is completely inhibited by CO, it is proposed that oxyhaemoglobin is oxidized after O2 dissociation, as has been suggested for the oxidation of oxyhaemoglobin by inorganic complexes. From the present analysis, ferricytochrome b5 seems unlikely to contribute significantly to methaemoglobin formation in vivo. Nevertheless, this observation provides a relatively convenient means of investigating the mechanism by which these two proteins interact.
已发现高铁细胞色素b5在先前发现的有利于高铁细胞色素b5与高铁血红蛋白形成复合物的最佳条件下,可将氧合血红蛋白转化为高铁血红蛋白[莫克和莫克(1982年)《生物化学》21卷,4730 - 4734页]。由于该反应完全被一氧化碳抑制,因此有人提出,氧合血红蛋白在氧气解离后被氧化,这与无机复合物对氧合血红蛋白的氧化情况一致。从目前的分析来看,高铁细胞色素b5似乎不太可能在体内显著促进高铁血红蛋白的形成。然而,这一观察结果为研究这两种蛋白质相互作用的机制提供了一种相对便捷的方法。