Alfsen A, Bade D, Bürck U, Eicher H, Formanek S, Kalvius G M, Lavialle F, Mayer A, Parak F, Tejada J, Thomanek U F
Biophys Struct Mech. 1977 Sep 28;3(3-4):229-38. doi: 10.1007/BF00535698.
Haemoglobin Haptoglobin complexes formed when [Hp+]/[Hb]= 1/1 and [Hp]/[Hb] =2/1 were investigated by 57Fe Mössbauer spectroscopy. Both samples gave a spectrum consisting of a single quadrupole doublet. The temperature dependence of the quadrupole splitting was also identical for both samples. This proves that in both samples the nearest neighbour environment of the iron atom must be the same. A comparison with earlier investigations on myoglobin and haemoglobin indicates that the electronic structure of iron in the HbHp-complexes is similar to that in myoglobin.
通过57Fe穆斯堡尔光谱研究了当[Hp+]/[Hb]=1/1和[Hp]/[Hb]=2/1时形成的血红蛋白-触珠蛋白复合物。两个样品都给出了由单个四极双峰组成的光谱。两个样品的四极分裂的温度依赖性也相同。这证明在两个样品中，铁原子的最近邻环境一定是相同的。与早期对肌红蛋白和血红蛋白的研究比较表明，血红蛋白-触珠蛋白复合物中铁的电子结构与肌红蛋白中的相似。
