LEENE W
J Cell Biol. 1964 Mar;20(3):377-87. doi: 10.1083/jcb.20.3.377.
In order to obtain information on the exact location of the respiratory enzyme chain in Gram-negative bacteria, an electron microscopic study was made of the sites of reducing activity of cells that had, in the living state, incorporated tellurite. In the test object Proteus vulgaris, the reduced tellurite was found to be deposited in bodies contiguous with the plasma membrane but different in structure from those described in the Gram-positive Bacillus subtilis (2). In fact, the bodies proved to consist of a conglomerate of elements which contained the strongly electron-scattering reduced tellurite and a delicately granular "matrix." A limiting membrane was not observed around these complexes. In serial sections details of the complexes are illustrated. Reduced tellurite was not deposited in the plasma membrane to any important degree. Since no other sites of deposition of the reduced product were revealed, it is assumed that the complexes represent the mitochondrial equivalents in the investigated organism. In addition, the bodies might function as the basal granules of the flagella.
为了获取革兰氏阴性菌中呼吸酶链的确切位置信息，对在活态下摄入亚碲酸盐的细胞的还原活性位点进行了电子显微镜研究。在测试对象普通变形杆菌中，发现还原的亚碲酸盐沉积在与质膜相邻但结构不同于革兰氏阳性枯草芽孢杆菌中所描述的那些结构的小体中。实际上，这些小体被证明是由含有强电子散射的还原亚碲酸盐和精细颗粒状“基质”的元素聚集体组成。在这些复合物周围未观察到限制膜。在连续切片中展示了复合物的细节。还原的亚碲酸盐在质膜中没有大量沉积。由于未发现还原产物的其他沉积位点，因此假定这些复合物代表所研究生物体中的线粒体等价物。此外，这些小体可能充当鞭毛的基部颗粒。
