Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S -: Implications for interactions of nitric oxide with normal and sickle red blood cells
Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S -: Implications for interactions of nitric oxide with normal and sickle red blood cells
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DOI：
10.1074/jbc.m107658200
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发表时间：
2002-04-26
影响因子：
4.8
通讯作者：
Crumbliss, AL
中科院分区：
文献类型：
--
作者：
Bonaventura, C;Taboy, CH;Crumbliss, AL
S-亚硝化血红蛋白是非常稳定的，可以循环之间的脱氧，氧合，或氧化的形式没有显着损失的NO。在这里，我们表明，S-亚硝化成人血红蛋白（血红蛋白A（0））或镰状细胞血红蛋白（血红蛋白S）的结果在增加的厌氧血红素氧化的容易性，而阴离子导致氧化还原转变在相反的方向。带3蛋白质的胞质结构域的带负电荷的基团也对S-亚硝化Hb产生变构效应。SNO-Hb/Band 3蛋白组装体的形成和脱氧本身不会导致NO释放，即使在谷胱甘肽存在的情况下也是如此;然而，该组装体可能在NO从红细胞迁移到其他靶点中起作用，并且可能与海因茨小体形成有关。对Hb S厌氧氧化的研究表明，相对于Hb A（0），氧化还原电位发生了改变，这有利于高铁血红蛋白的形成，因此可能是Hb S在有氧条件下自氧化速率增加、镰状细胞中海因茨小体形成增加以及含Hb S的红细胞寿命缩短的基础。一个模型之间的相互关系脱氧，氧，甲硫氨酸形式的血红蛋白A（0）和血红蛋白S，和他们的S-亚硝化对应物，提出。
S-Nitrosated hemoglobin is remarkably stable and can be cycled between deoxy, oxygenated, or oxidized forms without significant loss of NO. Here we show that S-nitrosation of adult human hemoglobin (Hb A(0)) or sickle cell Hb (Hb S) results in an increased ease of anaerobic heme oxidation, while anions cause redox shifts in the opposite direction. The negatively charged groups of the cytoplasmic domain of Band 3 protein also produce an allosteric effect on S-nitrosated Hb. Formation and deoxygenation of a SNO-Hb/Band 3 protein assembly does not in itself cause NO release, even in the presence of glutathione; however, this assembly may play a role in the migration of NO from the red blood cells to other targets and may be linked to Heinz body formation. Studies of the anaerobic oxidation of Hb S revealed an altered redox potential relative to Hb A(0) that favors met-Hb formation and may therefore underlie the increased rate of autoxidation of Hb S under aerobic conditions, the increased formation of Heinz bodies in sickle cells, and the decreased lifetime of red cells containing Hb S. A model for the interrelationships between the deoxy, oxy, and met forms of Hb A(0) and Hb S, and their S-nitrosated counterparts, is presented.