Submicromolar Ag+ increases passive Na+ permeability and inhibits the respiration‐supported formation of Na+ gradient in Bacillus FTU vesicles
- 20 August 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 269 (1), 69-72
- https://doi.org/10.1016/0014-5793(90)81120-d
Abstract
The effect of Ag+ on Na+ pumping by Na+‐motive NADH‐quinone reductase and terminal oxidase has been studied in Bacillus FTU inside‐out vesicles. Very low concentrations of Ag+ (C = 1 × 10−8M or 2 × 10−12 g ion · mg protein−1) are shown to inhibit the uphill Na+ uptake coupled to the oxidation of NADH by fumarate or of ascorbate + TMPD by oxygen but exert no effect on the H+ uptake by the H+‐motive respiratory chain. Low Ag+ also induces a specific increase in the Na+ permeability of the vesicles. HQNO, added before and not after Ag+, prevents the Ag+‐induced permeability increase, with effective HQNO concentrations being similar to those inhibiting the uphill Na+‐uptake coupled to the NADH‐fumarate oxidoreduction. Reduction of terminal oxidase by ascorbate + TMPD in the presence of cyanide sensitizes the Na+ permeability to Ag+. It is suggested that low [Ag+], known as a specific inhibitor of electron transport by the Na+‐motive NADH‐quinone reductase, uncouples the electron and Na+ transports so that the Ag+‐modified NADH‐quinone reductase operates as an Na+ channel rather than an Na+ pump. This effect is discussed in connection with the antibacterial action of Ag+.
Keywords
This publication has 5 references indexed in Scilit:
- The Na+ ‐motive terminal oxidase activity in an alkalo‐ and halo‐tolerant BacillusEuropean Journal of Biochemistry, 1989
- Membrane BioenergeticsPublished by Springer Science and Business Media LLC ,1988
- Ag+-sensitive NADH dehydrogenase in the Na+-motive respiratory chain of the marine bacterium Vibrio alginolyticus.Agricultural and Biological Chemistry, 1985
- Characterization of the respiration-dependent Na+ pump in the marine bacterium Vibrio alginolyticus.Journal of Biological Chemistry, 1982
- Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase.Journal of Biological Chemistry, 1977