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J Bacteriol. 1972 August; 111(2): 525-530
Copyright © 1972 American Society for Microbiology. All Rights Reserved.
a Laboratory of Molecular Biology, National Institute of Neurological Diseases and Stroke, Bethesda, Maryland 20014
ABSTRACT
Acetate and other short chain n-fatty acids (C1-C6) inhibit strongly the uptake of L-serine or other L-amino acids but inhibit only weakly that of
-methylglucoside or fructose, whether measured in whole cells of Bacillus subtilis or in membrane vesicles that have been energized with reduced nicotinamide adenine dinucleotide (NADH), L-
-glycerol phosphate, or ascorbate plus phenazine methosulfate. The acetate inhibition is noncompetitive, as was shown for L-
-aminoisobutyric acid uptake by whole cells and for L-serine uptake by membrane vesicles. In membrane preparations, neither NADH oxidation nor the reduction of cytochromes by NADH are affected by fatty acids. All of these effects are similar to those of 2, 4-dinitrophenol. It is concluded that the fatty acids "uncouple" the amino acid carrier proteins from the cytochrome-linked electron transport system (to which they may be coupled via protein interaction or via a cation gradient).
1 Present address: Laboratory for Microbiology, University of Groningen, The Netherlands.
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