Tsuprun V L, Mitsova I Z, Blazhchuk I S, Gvozdev R I, Orlova E V, Kiselev N A
Eur J Biochem. 1985 Jun 3;149(2):389-92. doi: 10.1111/j.1432-1033.1985.tb08937.x.
The quaternary structure of the Mo-Fe-protein from Azotobacter vinelandii has been studied by electron microscopy. A model of the molecule of the Mo-Fe-protein has been proposed: two alpha subunits are displaced relative to two beta subunits along a twofold axis, so the molecule can be characterized by the point-group pseudosymmetry 222. Computer averaging of the images showed that one of the projections of the molecule could be characterized by twofold rotational symmetry. Micrographs of nitrogenase recombined complex (Mo-Fe-protein + Fe-protein) have been obtained. They showed particles close in size and form to the Mo-Fe-protein molecule. Therefore, it has been proposed that the Fe-protein could be situated in the central cavity of Mo-Fe-protein.
通过电子显微镜研究了棕色固氮菌钼铁蛋白的四级结构。提出了钼铁蛋白分子模型：两个α亚基相对于两个β亚基沿二重轴发生位移，因此该分子可由点群假对称222表征。图像的计算机平均显示，该分子的一个投影可由二重旋转对称表征。已获得固氮酶重组复合物（钼铁蛋白+铁蛋白）的显微照片。它们显示出大小和形状与钼铁蛋白分子相近的颗粒。因此，有人提出铁蛋白可能位于钼铁蛋白的中心腔内。
