We showed previously that the outer membrane of the Escherichia coli cell envelope normally contains about 200 to 250 B12 receptors, and that these receptors function both in B12 transport and as receptors for the E colicins. This paper shows that this receptor system is also shared with bacteriophage BF23. A strong positive correlation was observed between the number of B12 receptors per cell and the rate of adsorption of BF23. Cells from mutant strains that lacked B12 receptors did not adsorb BF23 particles. The rate of adsorption of BF23 to cells of a merodiploid strain (RK4151), with about 550 B12 receptors per cell, was approximately double that to cells of a nonnal, haploid strain. The adsorption of BF23 to whole cells, cell envelopes, outer membrane particles, and solubilized outer membranes was inhibited by vitamin B12, with 50% inhibition at B12 concentrations in the range of 0.5 to 2.0 nM. These values are close to the 1032 on August 5, 2020 by guest
This paper presents some evidence that the osmotic shock-sensitive, energydependent transfer of vitamin B,2 from outer membrane receptor sites into the interior of cells of Escherichia coli requires an energized inner membrane, without obligatory intermediation of adenosine 5'-triphosphate (ATP). The experiments measured the effects of glucose, i>lactate, anaerobiosis, arsenate, cyanide, and 2,4-dinitrophenol upon the rates of B12 transport by starved cells of E. coli KBT001, which possesses a functional Ca2 , Mg2+-stimulated adenosine triphosphatase (Ca,MgATPase), and ofE. coli AN120, which lacks this enzyme. Both strains were able to utilize glucose and-lactate aerobically to potentiate B12 transport, indicating that the Ca,MgATPase was not essential for this process. When respiratory electron transport was blocked, either by cyanide or by anaerobic conditions, and the primary source of energy for the cells was presumably ATP from glucose fermentation, the rate of B12 transport was much reduced in E. coli AN120 but not in E. coli KBT001. These results support the view that the Ca,MgATPase can play a role in B12 transport but only when the energy for this process must be derived from ATP. The results of experiments with arsenate also supported the conclusion that the generation of phosphate bond energy was not absolutely required for B12 transport.
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