Abstract
Membrane vesicles of Veillonella alcalescens, grown in the presence of L-lactate and KNO-3, actively transport amino acids under anaerobic conditions in the presence of several electron donors and the electron acceptor nitrate. The highest initial rates of uptake are obtained with L-lactate, followed by reduced nicotinamide adenine dinucleotide, glycerol-1-phosphate, formate, and L-malate.. The membrane vesicles contain the dehydrogenases for these electron donors, and these enzymes are coupled with nitrate reductase. In membrane vesicles from cells, grown in the presence of nitrate, the dehydrogenases are not coupled with fumarate reducatase, and anaerobic transport of amino acids does not occur with fumarate as electron acceptor. Under aerobic conditions none of the physiological electron donors can energize transport. However, a high rate of uptake is observed with the electron donor system ascorbate-phenazine metho-sulfate. This electron donor system also effectively energizes transport under anaerobicconditions in the presence of the electron acceptor nitrate.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Enoch H. G., Lester R. L. Effects of molybdate, tungstate, and selenium compounds on formate dehydrogenase and other enzyme systems in Escherichia coli. J Bacteriol. 1972 Jun;110(3):1032–1040. doi: 10.1128/jb.110.3.1032-1040.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harold F. M. Conservation and transformation of energy by bacterial membranes. Bacteriol Rev. 1972 Jun;36(2):172–230. doi: 10.1128/br.36.2.172-230.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kistler W. S., Lin E. C. Anaerobic L- -glycerophosphate dehydrogenase of Escherichia coli: its genetic locus and its physiological role. J Bacteriol. 1971 Dec;108(3):1224–1234. doi: 10.1128/jb.108.3.1224-1234.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Konings W. N., Barnes E. M., Jr, Kaback H. R. Mechanisms of active transport in isolated membrane vesicles. 2. The coupling of reduced phenazine methosulfate to the concentrative uptake of beta-galactosides and amino acids. J Biol Chem. 1971 Oct 10;246(19):5857–5861. [PubMed] [Google Scholar]
- Konings W. N., Bisschop A., Daatselaar M. C.C. Transport of L-glutamate and L-aspartate by membrane vesicles of Bacillus subtilis W 23. FEBS Lett. 1972 Aug 15;24(3):260–264. doi: 10.1016/0014-5793(72)80368-5. [DOI] [PubMed] [Google Scholar]
- Konings W. N., Bisschop A., Veenhuis M., Vermeulen C. A. New procedure for the isolation of membrane vesicles of Bacillus subtilis and an electron microscopy study of their ultrastructure. J Bacteriol. 1973 Dec;116(3):1456–1465. doi: 10.1128/jb.116.3.1456-1465.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Konings W. N., Freese E. Amino acid transport in membrane vesicles of Bacillus subtilis. J Biol Chem. 1972 Apr 25;247(8):2408–2418. [PubMed] [Google Scholar]
- Konings W. N., Kaback H. R. Anaerobic transport in Escherichia coli membrane vesicles. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3376–3381. doi: 10.1073/pnas.70.12.3376. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Lester R. L., DeMoss J. A. Effects of molybdate and selenite on formate and nitrate metabolism in Escherichia coli. J Bacteriol. 1971 Mar;105(3):1006–1014. doi: 10.1128/jb.105.3.1006-1014.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matin A., Konings W. N. Transport of lactate and succinate by membrane vesicles of Escherichia coli, Bacillus subtilis and a pseudomonas species. Eur J Biochem. 1973 Apr 2;34(1):58–67. doi: 10.1111/j.1432-1033.1973.tb02728.x. [DOI] [PubMed] [Google Scholar]
- Miki K., Lin E. C. Enzyme complex which couples glycerol-3-phosphate dehydrogenation to fumarate reduction in Escherichia coli. J Bacteriol. 1973 May;114(2):767–771. doi: 10.1128/jb.114.2.767-771.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ruiz-Herrera J., Showe M. K., DeMoss J. A. Nitrate reductase complex of Escherichia coli K-12: isolation and characterization of mutants unable to reduce nitrate. J Bacteriol. 1969 Mar;97(3):1291–1297. doi: 10.1128/jb.97.3.1291-1297.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Showe M. K., DeMoss J. A. Localization and regulation of synthesis of nitrate reductase in Escherichia coli. J Bacteriol. 1968 Apr;95(4):1305–1313. doi: 10.1128/jb.95.4.1305-1313.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spencer M. E., Guest J. R. Isolation and properties of fumarate reductase mutants of Escherichia coli. J Bacteriol. 1973 May;114(2):563–570. doi: 10.1128/jb.114.2.563-570.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- de Vries W., van Wijck-Kapteyn W. M., Oosterhuis S. K. The presence and function of cytochromes in Selenomonas ruminantium, Anaerovibrio lipolytica and Veillonella alcalescens. J Gen Microbiol. 1974 Mar;81(1):69–78. doi: 10.1099/00221287-81-1-69. [DOI] [PubMed] [Google Scholar]
- de Vries W., van Wyck-Kapteyn W. M., Stouthamer A. H. Generation of ATP during cytochrome-linked anaerobic electron transport in propionic acid bacteria. J Gen Microbiol. 1973 May;76(1):31–41. doi: 10.1099/00221287-76-1-31. [DOI] [PubMed] [Google Scholar]