NDLI: Energy transduction in the thermophilic anaerobic bacterium Clostridium fervidus is exclusively coupled to sodium ions.

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Energy transduction in the thermophilic anaerobic bacterium Clostridium fervidus is exclusively coupled to sodium ions.

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Energy transduction in the thermophilic anaerobic bacterium Clostridium fervidus is exclusively coupled to sodium ions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Speelmans, G. Abee, T. Poolman, B. Konings, W. N.
Description	Author Affiliation: Speelmans G ( Department of Microbiology, University of Groningen, Haren, The Netherlands.);
Abstract	The thermophilic, peptidolytic, anaerobic bacterium Clostridium fervidus is unable to generate a pH gradient in the range of 5.5-8.0, which limits growth of the organism to a narrow pH range (6.3-7.7). A significant membrane potential (delta psi approximately -60 mV) and chemical gradient of Na+ (-Z delta pNa approximately -60 mV) are formed in the presence of metabolizable substrates. Energy-dependent Na+ efflux is inhibited by the Na+/H+ ionophore monensin but is stimulated by uncouplers, suggesting that the Na+ gradient is formed by a primary pumping mechanism rather than by secondary Na+/H+ antiport. This primary sodium pump was found to be an ATPase that has been characterized in inside-out membrane vesicles and in proteoliposomes in which solubilized ATPase was reconstituted. The enzyme is stimulated by Na+, resistant to vanadate, and sensitive to nitrate, which is indicative of an F/V-type Na(+)-ATPase. In the proteoliposomes Na+ accumulation depends on the presence of ATP, is inhibited by the ATPase inhibitor nitrate, and is completely prevented by the ionophore monensin but is stimulated by protonophores and valinomycin. These and previous observations, which indicated that secondary amino acid transport uses solely Na+ as coupling ion, demonstrate that energy transduction at the membrane in C. fervidus is exclusively dependent on a Na+ cycle.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphatases Metabolism Clostridium Sodium Pharmacology Amino Acids Anaerobiosis Cell Membrane Drug Effects Growth & Development Energy Metabolism Hot Temperature Hydrogen-Ion Concentration Kinetics Liposomes Membrane Potentials Models, Biological Monensin Proteolipids Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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