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Chemomechanical Coupling without ATP: The Source of Energy for Motility and Chemotaxis in Bacteria

by: Steven H Larsen, Julius Adler, Jay J Gargus, Robert W Hogg
Proceedings of the National Academy of Sciences, Vol. 71, No. 4. (15 April 1974), pp. 1239-1243.


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The source of energy for bacterial motility is the intermediate in oxidative phosphorylation, not ATP directly. For chemotaxis, however, there is an additional requirement, presumably ATP. These conclusions are based on the following findings. (i) Unlike their parents, mutants of Escherichia coli and Salmonella typhimurium that are blocked in the conversion of ATP to the intermediate of oxidative phosphorylation failed to swim anaerobically, even when they produced ATP. When respiration was restored to the mutants, motility was simultaneously restored. (ii) Carbonylcyanide m-chlorophenyl-hydrazone, which uncouples oxidative phosphorylation, completely inhibited motility even though ATP remained present. (iii) Arsenate did not inhibit motility in the presence of an oxidizable substrate, though it did reduce ATP levels to less than 0.3%. (iv) Arsenate completely inhibited chemotaxis under conditions where motility was normal. 10.1073/pnas.71.4.1239


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