This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Boonstra, J. Articles by Konings, W. N. Search for Related Content PubMed PubMed Citation Articles by Boonstra, J. Articles by Konings, W. N.

 Previous Article  |  Next Article 

J Bacteriol. 1978 December; 136(3): 844-853
Copyright © 1978 American Society for Microbiology. All Rights Reserved.

Energy Supply for Active Transport in Anaerobically Grown Escherichia coli

Johannes Boonstra^1,, J. Allan Downie² and Wil N. Konings¹

¹ Department of Microbiology, Biological Centre, 9751 NN Haren, The Netherlands
² Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra A.C.T., Australia

ABSTRACT

Escherichia coli K-12, grown under anaerobic conditions with glucose as the sole source of carbon and energy without any terminal electron acceptor added, contains a fumarate reductase system in which electrons are transferred from formate or reduced nicotinamide adenine dinucleotide via menaquinone and cytochromes to fumarate reductase. This fumarate reductase system plays an important role in the metabolic energy supply of E. coli, grown under so-called "glycolytic conditions," as is indicated by the growth yields and maximal growth rates of mutants impaired in electron transfer or adenosine triphosphatase (uncB). In mutants deficient in menaquinone, cytochromes, or fumarate reductase, these values are considerably lower than in mutants deficient in ubiquinone or a functional adenosine triphosphatase. Electron transfer in this fumarate reductase system leads to the generation of a membrane potential, as is indicated by the uptake of the lipophilic cation triphenylmethylphosphonium by membrane vesicles prepared from cytochrome-sufficient and uncB cells. The generation of a proton-motive force by the fumarate reductase system was also demonstrated by the uptake of amino acids under anaerobic conditions in membrane vesicles of cytochrome containing and uncB cells grown under glycolytic conditions. Membrane vesicles of cytochrome-deficient cells failed to accumulate triphenyl-methylphosphonium and amino acids under these conditions, indicating that cytochromes are essential for the generation of a proton-motive force. Using glutamine uptake as an indication of the generation of ATP and proline uptake as an indication of the generation of a proton-motive force, it was demonstrated in whole cells that the proton-motive force is formed by ATP hydrolysis in cytochrome-deficient cells and by electron transfer in the uncB cells. In cytochrome-containing cells it was not possible to distinguish between these two possibilities, but the growth parameters suggest that, under glycolytic conditions, the proton-motive force is generated via electron transfer in the fumarate reductase system rather than via ATP hydrolysis.

Present address: Hubrecht Laboratory, De Uithof, 3584 CT Utrecht, The Netherlands.

This article has been cited by other articles:

• Buettner, F. F. R., Bendallah, I. M., Bosse, J. T., Dreckmann, K., Nash, J. H. E., Langford, P. R., Gerlach, G.-F. (2008). Analysis of the Actinobacillus pleuropneumoniae ArcA Regulon Identifies Fumarate Reductase as a Determinant of Virulence. Infect. Immun. 76: 2284-2295 [Abstract] [Full Text]