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PMID: 2387416 Published · ppublish English Journal Article

Submicromolar Ag+ increases passive Na+ permeability and inhibits the respiration-supported formation of Na+ gradient in Bacillus FTU vesicles.

FEBS letters ·Vol. 269 ·No. 1 ·1990-08-20 ·Pages 69-72

Semeykina AL, Skulachev VP

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+ (C1/2 = 1 x 10(-8) M or 2 x 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+.

MeSH Terms
Bacillus/drug effects,physiology Biological Transport, Active/drug effects Cations, Monovalent Cell Membrane Permeability/drug effects Cell-Free System Energy Metabolism/drug effects Hydroxyquinolines/pharmacology In Vitro Techniques Membrane Potentials/drug effects Quinone Reductases/metabolism Silver/pharmacology Sodium/metabolism
Chemicals
Cations, Monovalent Hydroxyquinolines 2-(n-heptyl)-4-hydroxyquinoline N-oxide Silver Sodium NADH dehydrogenase (quinone) Quinone Reductases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Semeykina A L
Department of Bioenergetics, A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Skulachev V P
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1990-08-20
Pages
69-72
Language
English
Region
England
NLM ID
0155157
Subset
IM
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