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F Gibson

Publications and source records attributed to F Gibson.

At least 145 records · Page 8Linked to original sources

The function of ubiquinone in Escherichia coli.

1. The function of ubiquinone in Escherichia coli was studied by using whole cells and membrane preparations of normal E. coli and of a mutant lacking ubiquinone. 2. The mutant lacking ubiquinone, strain AN59 (Ubi(-)), when grown under aerobic conditions, gave an anaerobic type of growth yield and produced large quantities of lactic acid, indicating that ubiquinone plays a vital role in electron transport. 3. NADH and lactate oxidase activities in membranes from strain AN59 (Ubi(-)) were greatly impaired and activity was restored by the addition of ubiquinone (Q-1). 4. Comparison of the percentage reduction of flavin, cytochrome b(1) and cytochrome a(2) in the aerobic steady state in membranes from the normal strain (AN62) and strain AN59 (Ubi(-)) and the effect of respiratory inhibitors on these percentages in membranes from strain AN62 suggest that ubiquinone functions at more than one site in the electron-transport chain. 5. Membranes from strain AN62, in the absence of substrate, showed an electron-spin-resonance signal attributed to ubisemiquinone. The amount of reduced ubiquinone (50%) found after rapid solvent extraction is consistent with the existence of ubiquinone in membranes as a stabilized ubisemiquinone. 6. The effects of piericidin A on membranes from strain AN62 suggest that this inhibitor acts at the ubiquinone sites: thus inhibition of electron transport is reversed by ubiquinone (Q-1); the aerobic steady-state oxidation-reduction levels of flavins and cytochrome b(1) in the presence of the inhibitor are raised to values approximating those found in the membranes of strain AN59 (Ubi(-)); the inhibitor rapidly eliminates the electron-spin-resonance signal attributed to ubisemiquinone and allows slow oxidation of endogenous ubiquinol in the absence of substrate and prevents reduction of ubiquinone in the presence of substrate. It is concluded that piericidin A separates ubiquinone from the remainder of the electron-transport chain. 7. A scheme is proposed in which ubisemiquinone, complexed to an electron carrier, functions in at least two positions in the electron-transport sequence.

Amobarbital↗

Biosynthesis of 4-aminobenzoate in Escherichia coli.

Two different mutations (pabA and pabB) affecting 4-aminobenzoate biosynthesis were obtained in strains of Escherichia coli lacking chorismate mutase and anthranilate synthetase activity, thus allowing study of the pathway of biosynthesis of 4-aminobenzoate by use of cell extracts of strains carrying the pab mutations. Two components with approximate molecular weights of 9,000 (component A) and 48,000 (component B) are concerned in the biosynthesis of 4-aminobenzoate from chorismate by E. coli. No diffusible intermediate compound could be detected.

Aminobenzoates↗

Mutations affecting iron transport in Escherichia coli.

A mutant of Escherichia coli K-12 unable to form an essential component of the enterochelin-dependent iron transport system has been isolated. This strain carries a mutation in a gene designated fep, mapping close to two genes, entA and entD, concerned with enterochelin synthesis. Strain AN102, which carries the fep(-) allele, accumulates large quantities of enterochelin and gives a growth response to sodium citrate. The cytochrome b(1) and total iron content, and the measurement of the uptake of (55)Fe(3+), indicate an impairment of the enterochelin-dependent iron transport system. The growth response to sodium citrate is related to the presence, in strain AN102, of an inducible citrate-dependent iron transport system.

Biological Transport↗

Biosynthesis of ubiquinone in Escherichia coli K-12: location of genes affecting the metabolism of 3-octaprenyl-4-hydroxybenzoic acid and 2-octaprenylphenol.

Two genes (ubiB and ubiD) concerned with two successive reactions in ubiquinone biosynthesis in Escherichia coli were mapped and found to be closely linked. Mutant strains of E. coli carrying the ubiB(-) and ubiD(-) alleles were shown to accumulate 2-octaprenylphenol and 3-octaprenyl-4-hydroxybenzoic acid, respectively. These compounds were isolated and identified by using nuclear magnetic resonance and mass and infrared spectroscopy. Cell extracts from the mutant strain carrying the ubiD(-) allele lack 3-octaprenyl-4-hydroxybenzoate decarboxylase activity.

Benzoates↗

Mutant strains of Escherichia coli K-12 unable to form ubiquinone.

A strain of Escherichia coli was isolated which was unable to form ubiquinone. This mutant was obtained by selecting strains unable to grow on malate as sole source of carbon. Such strains were further screened by examination of the quinone content of cells grown on a glucose medium. A mutant unable to form vitamin K was also isolated by this procedure. A genetic analysis of the ubiquinoneless strain showed that it possessed two mutations affecting ubiquinone biosynthesis.

Chromatography↗