过氧化氢作用下血红蛋白亚基形成高铁血红素。
Haemichrome formation from haemoglobin subunits by hydrogen peroxide.
作者信息
Tomoda A, Sugimoto K, Suhara M, Takeshita M, Yoneyama Y
出版信息
Biochem J. 1978 May 1;171(2):329-35. doi: 10.1042/bj1710329.
The effect of H2O2 on ferrous human haemoglobin subunits (alphash-, betash-, alphapmb- and betapmb-chains) was studied. These chains were easily transformed to haemichrome by the addition of H2O2 or H2O2-generating systems, including glucose oxidase (EC 1.1.3.4) AND XANTHINE OXIDASE (EC 1.2.3.2), and this was ascertained by e.p.r. measurements and by absorption spectra. The changes in these haemoglobin subunits were not inhibited by superoxide dismutase (EC 1.15.1.1), but were decreased by catalase (EC 1.11.1.6). The rate of oxidation of alphapmb-chains was higher than that of alphash-chains, and the rate of oxidation of betapmb-chains was higher than that of betash-chains. Haemichrome was demonstrated to be formed directly from these ferrous chains by the attack by H2O2, and this process did not involve formation of methaemoglobin. On the basis of these findings the kinetics of the reaction between the haemoglobin subunits and H2O2 was studied, and the pathological significance of H2O2 in disorders of erythrocytes such as thalassaemia was discussed.
研究了过氧化氢对人血红蛋白亚铁亚基（α链、β链、α链和β链）的影响。通过添加过氧化氢或产生过氧化氢的系统，包括葡萄糖氧化酶（EC 1.1.3.4）和黄嘌呤氧化酶（EC 1.2.3.2），这些亚基很容易转化为高铁血红素，这通过电子顺磁共振测量和吸收光谱得以确定。这些血红蛋白亚基的变化不受超氧化物歧化酶（EC 1.15.1.1）的抑制，但过氧化氢酶（EC 1.11.1.6）可使其降低。α链的氧化速率高于α链，β链的氧化速率高于β链。已证明高铁血红素是由过氧化氢攻击这些亚铁链直接形成的，且该过程不涉及高铁血红蛋白的形成。基于这些发现，研究了血红蛋白亚基与过氧化氢反应的动力学，并讨论了过氧化氢在地中海贫血等红细胞疾病中的病理意义。
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