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Mechanisms of Sodium Transport in Bacteria
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
Vol. 326, No. 1236, Microbial Membrane Transport Systems (Jan. 30, 1990), pp. 465-477
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/2398759
Page Count: 13
You can always find the topics here!Topics: Adenosine triphosphatases, Ions, Enzymes, Pumps, Citrates, Protons, Bacteria, Sodium, Decarboxylation, Fermentation
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In some bacteria, an Na+ circuit is an important link between exergonic and endergonic membrane reactions. The physiological importance of Na+ ion cycling is described in detail for three different bacteria. Klebsiella pneumoniae fermenting citrate pumps Na+ outwards by oxaloacetate decarboxylase and uses the Na+ ion gradient thus established for citrate uptake. Another possible function of the Na+ gradient may be to drive the endergonic reduction of NAD+ with ubiquinol as electron donor. In Vibrio alginolyticus, an Na+ gradient is established by the NADH: ubiquinone oxidoreductase segment of the respiratory chain; the Na+ gradient drives solute uptake, flagellar motion and possibly ATP synthesis. In Propionigenium modestum, ATP biosynthesis is entirely dependent on the Na+ ion gradient established upon decarboxylation of methylmalonyl-CoA. The three Na+-translocating enzymes, oxaloacetate decarboxylase of Klebsiella pneumoniae, NADH: ubiquinone oxidoreductase of Vibrio alginolyticus and ATPase (F1F0) of Propionigenium modestum have been isolated and studied with respect to structure and function. Oxaloacetate decarboxylase consists of a peripheral subunit (α), that catalyses the carboxyltransfer from oxaloacetate to enzyme-bound biotin. The subunits β and γ are firmly embedded in the membrane and catalyse the decarboxylation of the carboxybiotin enzyme, coupled to Na+ transport. A two-step mechanism has also been demonstrated for the respiratory Na+ pump. Semiquinone radicals are first formed with the electrons from NADH; subsequently, these radicals dismutate in an Na+-dependent reaction to quinone and quinol. The ATPase of P. modestum is closely related in its structure to the F1F0 ATPase of E. coli, but uses Na+ as the coupling ion. A specific role of protons in the ATP synthesis mechanism is therefore excluded.
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences © 1990 Royal Society