scholarly journals Anaerobic Growth of Escherichia coli K12 with Fumarate as Terminal Electron Acceptor. Genetic Studies with Menaquinone and Fluoroacetate-resistant Mutants

1979 ◽  
Vol 115 (2) ◽  
pp. 259-271 ◽  
Author(s):  
J. R. GUEST
1988 ◽  
Vol 34 (6) ◽  
pp. 822-824 ◽  
Author(s):  
Holly E. Richter ◽  
Jacek Switala ◽  
Peter C. Loewen

The addition of ascorbate to aerobically growing cultures of Escherichia coli B caused only a short pause in growth and no subsequent change in the rate or extent of growth. The effect of ascorbate on oxygen uptake varied from inhibition in minimal medium to stimulation in rich medium. Cyanide-resistant growth and oxygen uptake were stimulated by ascorbate. Both the rate and extent of anaerobic growth were stimulated in proportion to the amount of ascorbate added when fumarate was the terminal electron acceptor. Ascorbate had no effect on any aspect of anaerobic growth in the absence of a terminal electron acceptor or in the presence of nitrate.


2013 ◽  
Vol 63 (Pt_5) ◽  
pp. 1824-1833 ◽  
Author(s):  
Dennis A. Bazylinski ◽  
Timothy J. Williams ◽  
Christopher T. Lefèvre ◽  
Denis Trubitsyn ◽  
Jiasong Fang ◽  
...  

A magnetotactic bacterium, designated strain MV-1T, was isolated from sulfide-rich sediments in a salt marsh near Boston, MA, USA. Cells of strain MV-1T were Gram-negative, and vibrioid to helicoid in morphology. Cells were motile by means of a single polar flagellum. The cells appeared to display a transitional state between axial and polar magnetotaxis: cells swam in both directions, but generally had longer excursions in one direction than the other. Cells possessed a single chain of magnetosomes containing truncated hexaoctahedral crystals of magnetite, positioned along the long axis of the cell. Strain MV-1T was a microaerophile that was also capable of anaerobic growth on some nitrogen oxides. Salinities greater than 10 % seawater were required for growth. Strain MV-1T exhibited chemolithoautotrophic growth on thiosulfate and sulfide with oxygen as the terminal electron acceptor (microaerobic growth) and on thiosulfate using nitrous oxide (N2O) as the terminal electron acceptor (anaerobic growth). Chemo-organoautotrophic and methylotrophic growth was supported by formate under microaerobic conditions. Autotrophic growth occurred via the Calvin–Benson–Bassham cycle. Chemo-organoheterotrophic growth was supported by various organic acids and amino acids, under microaerobic and anaerobic conditions. Optimal growth occurred at pH 7.0 and 26–28 °C. The genome of strain MV-1T consisted of a single, circular chromosome, about 3.7 Mb in size, with a G+C content of 52.9–53.5 mol%.Phylogenetic analysis based on 16S rRNA gene sequences indicated that strain MV-1T belongs to the family Rhodospirillaceae within the Alphaproteobacteria , but is not closely related to the genus Magnetospirillum . The name Magnetovibrio blakemorei gen. nov., sp. nov. is proposed for strain MV-1T. The type strain of Magnetovibrio blakemorei is MV-1T ( = ATCC BAA-1436T  = DSM 18854T).


2002 ◽  
Vol 184 (14) ◽  
pp. 4044-4047 ◽  
Author(s):  
Angelique Walt ◽  
Michael L. Kahn

ABSTRACT In Escherichia coli, the use of carnitine as a terminal electron acceptor depends on a functional caiTABCDE operon. It had been suggested that the adjacent but divergent fixABCX operon is also required for carnitine metabolism, perhaps to provide electrons for carnitine reduction. We have constructed E. coli fixA and fixB mutants and find that they are unable to reduce carnitine to γ-butyrobetaine under anaerobic conditions.


2001 ◽  
Vol 355 (1) ◽  
pp. 51-58 ◽  
Author(s):  
Eleanor REID ◽  
Jeff COLE ◽  
Deborah J. EAVES

In Escherichia coli K-12, c-type cytochromes are synthesized only during anaerobic growth with trimethylamine-N-oxide, nitrite or low concentrations of nitrate as the terminal electron acceptor. A thioredoxin-like protein, CcmG, is one of 12 proteins required for their assembly in the periplasm. Its postulated function is to reduce disulphide bonds formed between correctly paired cysteine residues in the cytochrome c apoproteins prior to haem attachment by CcmF and CcmH. We report that loss of CcmG synthesis by mutation was not compensated by a second mutation in disulphide-bond-forming proteins, DsbA or DsbB, or by the chemical reductant, 2-mercaptoethanesulphonic acid. An anti-CcmG polyclonal antibody was used in Western-blot analysis to probe the redox state of CcmG in mutants defective in the synthesis of other proteins essential for cytochrome c assembly. The oxidized form of CcmG accumulated not only in trxA or dipZ mutants defective in the transfer of electrons from the cytoplasm for disulphide isomerization and reduction reactions in the periplasm, but also in ccmF and ccmH mutants. The requirement of both CcmF and CcmH for the reduction of the disulphide bond in CcmG indicates that CcmG functions later than CcmF and CcmH in cytochrome c assembly, rather than in electron transfer from the membrane-associated DipZ (also known as DsbD) to CcmH. The data support a model proposed by others in which CcmG catalyses one of the last reactions specific to cytochrome c assembly.


1973 ◽  
Vol 127 (2) ◽  
pp. 175-189 ◽  
Author(s):  
H. G. Wittmann ◽  
G. Stöffler ◽  
D. Apirion ◽  
L. Rosen ◽  
K. Tanaka ◽  
...  

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