Tang Qian, Zheng Xue-Fang, Wang Jing-Yun, Liu Yuan-Yuan, Yuan Yu-Lian
Liaoning Key Lab of Bioorganic Chemistry, Dalian University, Dalian 116622, China.
Guang Pu Xue Yu Guang Pu Fen Xi. 2009 Jul;29(7):1958-61.
Myoglobin (Mb) made up of a multipeptides train and a heme prosthetic group is a kind of protein taking charge of O2 stock and distribution in mammal cells, especially in muscle cells. The heme-iron plays a key role in O2 transfer and transport. In the present paper, the direct interaction between heme-iron of myoglobin and additional metal ions [Cu (II), Zn (II) and Co( II)] was studied by UV-Vis spectra. It was found that heme-iron of myoglobin directly interacted with additional Cu(II), Zn(II) and Co(II), these metal ions could drag iron ion out from heme prosthetic group of myoglobin, and subsequently myoglobin became myoglobin derivatives lacking iron ion. At the same time, the effect of the additional metal ions concentration on the direction interaction was studied. It was shown that the direct interaction increased gradually with the amount of external metal ions added. When the ratio of Mb and metal ions is 1 : 10, the interaction intension between the three metal ions and Mb is Co(II), Zn(II) and Cu(II) in turn. For the first time, the authors confirmed that the direct interaction has occurred between heme-iron of myoglobin and additional metal ions, and saw about how the metal ions intension affects the direct interaction.
肌红蛋白（Mb）由一条多肽链和一个血红素辅基组成，是一种负责在哺乳动物细胞尤其是肌肉细胞中储存和分配氧气的蛋白质。血红素铁在氧气的传递和运输中起关键作用。在本文中，通过紫外可见光谱研究了肌红蛋白的血红素铁与额外金属离子[Cu（II）、Zn（II）和Co（II）]之间的直接相互作用。研究发现，肌红蛋白的血红素铁与额外的Cu（II）、Zn（II）和Co（II）直接相互作用，这些金属离子可将铁离子从肌红蛋白的血红素辅基中拽出，随后肌红蛋白变成缺乏铁离子的肌红蛋白衍生物。同时，研究了额外金属离子浓度对这种直接相互作用的影响。结果表明，直接相互作用随着外部添加金属离子量的增加而逐渐增强。当肌红蛋白与金属离子的比例为1∶10时，三种金属离子与肌红蛋白之间的相互作用强度依次为Co（II）、Zn（II）和Cu（II）。作者首次证实了肌红蛋白的血红素铁与额外金属离子之间发生了直接相互作用，并观察了金属离子强度如何影响这种直接相互作用。
