血红蛋白β亚基中一氧化氮从血红素到半胱氨酸缺乏变构控制的分子内转移。
Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the beta subunit of hemoglobin.
作者信息
Huang Kris T, Azarov Ivan, Basu Swati, Huang Jinming, Kim-Shapiro Daniel B
机构信息
Department of Biomedical Engineering, Wake Forest University, Winston-Salem, NC 27109, USA.
出版信息
Blood. 2006 Apr 1;107(7):2602-4. doi: 10.1182/blood-2005-10-4104. Epub 2005 Dec 8.
Abstract
The SNO-Hb hypothesis holds that heme-bound nitric oxide (NO) present in the beta subunits of T-state hemoglobin (Hb) will be transferred to the beta-93 cysteine upon conversion to R-state Hb, thereby forming SNO-Hb. A deficiency in the ability of Hb to facilitate this intramolecular transfer has recently been purported to play a role in pulmonary hypertension and sickle cell disease. We prepared deoxygenated Hb samples with small amounts of heme-bound NO and then oxygenated the samples. Electron paramagnetic resonance (EPR) spectroscopy was used to (1) determine the concentration of iron nitrosyl Hb (Fe-NO Hb), (2) show that the NO is evenly distributed among alpha and beta subunits, and (3) show that the Hb undergoes a change in its quaternary state (T to R) upon oxygenation. We did not observe a decrease in the concentration of Fe-NO Hb on oxygenation, which is inconsistent with the prediction of the SNO-Hb hypothesis.
摘要
SNO-Hb假说认为，处于T态血红蛋白（Hb）β亚基中的血红素结合型一氧化氮（NO）在转变为R态Hb时会转移至β-93位半胱氨酸，从而形成SNO-Hb。最近有人提出，Hb促进这种分子内转移的能力缺陷在肺动脉高压和镰状细胞病中起作用。我们制备了含有少量血红素结合型NO的脱氧Hb样品，然后对样品进行氧合。电子顺磁共振（EPR）光谱用于（1）测定铁亚硝酰Hb（Fe-NO Hb）的浓度，（2）表明NO在α和β亚基之间均匀分布，以及（3）表明Hb在氧合时其四级结构发生变化（从T态转变为R态）。我们未观察到氧合时Fe-NO Hb浓度降低，这与SNO-Hb假说的预测不一致。
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