R 态人血红蛋白一氧化氮衍生物的晶体学特征。
Crystallographic characterization of the nitric oxide derivative of R-state human hemoglobin.
机构信息
Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA; Department of Biological Engineering, Nanjing University of Science and Technology, Nanjing 210094, China.
Macromolecular Crystallography Research Resource, National Synchrotron Light Source, Brookhaven National Laboratory, Upton, NY 11973, USA.
出版信息
Nitric Oxide. 2014 May 30;39:46-50. doi: 10.1016/j.niox.2014.04.001. Epub 2014 Apr 22.
Nitric oxide (NO) is a signaling agent that is biosynthesized in vivo. NO binds to the heme center in human hemoglobin (Hb) to form the HbNO adduct. This reaction of NO with Hb has been studied for many decades. Of continued interest has been the effect that the bound NO ligand has on the geometrical parameters of the resulting heme-NO active site. Although the crystal structure of a T-state human HbNO complex has been published previously, that of the high affinity R-state HbNO derivative has not been reported to date. We have crystallized and solved the three-dimensional X-ray structure of R-state human HbNO to 1.90 Å resolution. The differences in the FeNO bond parameters and H-bonding patterns between the α and β subunits contribute to understanding of the observed enhanced stability of the α(FeNO) moieties relative to the β(FeNO) moieties in human R-state HbNO.
一氧化氮（NO）是一种在体内生物合成的信号剂。NO 与人类血红蛋白（Hb）中的血红素中心结合形成 HbNO 加合物。几十年来，人们一直在研究 NO 与 Hb 的这种反应。人们一直感兴趣的是，结合的 NO 配体对形成的血红素-NO 活性部位的几何参数的影响。尽管先前已经发表了 T 态人 HbNO 复合物的晶体结构，但迄今尚未报道高亲和力 R 态 HbNO 衍生物的晶体结构。我们已经结晶并解析了 R 态人 HbNO 的三维 X 射线结构，分辨率为 1.90Å。α 和β亚基中 FeNO 键参数和氢键模式的差异有助于理解在人 R 态 HbNO 中观察到的 α（FeNO）部分相对于 β（FeNO）部分的稳定性增强。
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