scholarly journals The molecular mechanisms of dicarboxylic acid transport in Escherichia coli K12. The role and orientation of the two membrane-bound dicarboxylate binding proteins

1978 ◽  
Vol 253 (21) ◽  
pp. 7826-7831
Author(s):  
T.C. Lo ◽  
M.A. Bewick
Keyword(s):  
Escherichia Coli ◽  
Dicarboxylic Acid ◽  
Binding Proteins ◽  
Molecular Mechanisms ◽  
Acid Transport ◽  
Escherichia Coli K12 ◽  
Membrane Bound

scholarly journals Succinate uptake and related proton movements in Escherichia coli K12

1975 ◽  
Vol 152 (3) ◽  
pp. 647-654 ◽  
Author(s):  
S J Gutowski ◽  
H Rosenberg
Keyword(s):  
Escherichia Coli ◽  
Dicarboxylic Acid ◽  
Transport System ◽  
Dicarboxylic Acids ◽  
Acid Transport ◽  
Cationic Form ◽  
Whole Cells ◽  
Escherichia Coli K12 ◽  
Proton Uptake

1. The apparent Km values for succinate uptake by whole cells of Escherichia coli K12 depend on pH in the range 6.5-7.4.2. Uptake of succinate in lightly buffered medium is accompanied by proton uptake. 3. The apparent Km values for succinate uptake and for succinate-induced proton uptake are similar. 4. Approximately two protons enter the cell with each succinate molecule. 5. The pattern of inhibition of succinate uptake is similar to that of succinate-induced proton uptake. 6. Uptake of fumarate and malate, which share the succinate-transport system, is also accompanied by the uptake of approximately two protons per molecule of fumarate or malate. 7. Uptake of aspartate by the dicarboxylic acid-transport system is accompanied by the uptake of approximatley two protons per molecule of asparatate. 8. It is concluded that uptake of dicarboxylic acids by the dicarboxylic acid-transport system is obligatorily coupled to proton uptake such that succinate, malate and fumarate are taken up in electroneutral form and asparate is taken up in cationic form. 9. These results are consistent with, though they do not definitely prove, the energization of succinate uptake of the deltapH.

scholarly journals Oxidative phosphorylation in Escherichia coli K12. An uncoupled mutant with altered membrane structure

1974 ◽  
Vol 138 (2) ◽  
pp. 211-215 ◽  
Author(s):  
G. B. Cox ◽  
F. Gibson ◽  
L. McCann
Keyword(s):  
Escherichia Coli ◽  
Electron Transport ◽  
Membrane Structure ◽  
Mutant Allele ◽  
Adenosine Triphosphatase ◽  
Mineral Salts ◽  
Normal Cells ◽  
E Coli ◽  
Escherichia Coli K12 ◽  
Membrane Bound

1. A new mutant strain (AN228) of Escherichia coli K12, unable to couple phosphorylation to electron transport, has been isolated. The mutant allele (unc-405), in strain AN228, was found to map near the uncA and uncB genes at about minute 74 on the E. coli genome. 2. A transductant strain (AN285) carrying the unc-405 allele is similar to the uncA and uncB mutants described previously in that it is unable to grow on succinate, gives a low aerobic yield on limiting concentrations of glucose, has a normal rate of electron transport, is unable to couple phosphorylation to electron transport, and lacks ATP-dependent transhydrogenase activity. 3. Strain AN285 (unc-405) is similar to an uncA mutant, but different from an uncB mutant, in that it is unable to grow anaerobically in a glucose–mineral-salts medium, and membrane preparations do not have Mg2+-stimulated adenosine triphosphatase activity. 4. Strain AN285 (unc-405) does not form an aggregate analogous to the membrane-bound Mg2+-stimulated adenosine triphosphatase aggregate found in normal cells. In this respect it differs from strain AN249 (uncA−), which forms an inactive membrane-bound Mg2+-stimulated adenosine triphosphatase aggregate.

scholarly journals Characterization of the membrane-bound nitrate reductase activity of aerobically grown chlorate-sensitive mutants of escherichia coli K12

FEBS Letters ◽  
1978 ◽  
Vol 95 (2) ◽  
pp. 290-294 ◽  
Author(s):  
Gérard Giordano ◽  
Alec Graham ◽  
David H. Boxer ◽  
Bruce A. Haddock ◽  
Edgard Azoulay
Keyword(s):  
Escherichia Coli ◽  
Nitrate Reductase ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Escherichia Coli K12 ◽  
Membrane Bound
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