scholarly journals Functional anaerobic electron transport linked to the reduction of nitrate and fumarate in membranes from Escherichia coli as demonstrated by quenching of atebrin fluorescence

1975 ◽  
Vol 152 (3) ◽  
pp. 655-659 ◽  
Author(s):  
B A Haddock ◽  
M W Kendall-Tobias
Keyword(s):  
Escherichia Coli ◽  
Electron Transport ◽  
Carbon Source ◽  
Electron Acceptor ◽  
Functional Organization ◽  
Terminal Electron Acceptor ◽  
Membrane Particles ◽  
Electron Transport Chains ◽  
Anaerobic Electron Transport ◽  
Energy Dependent

Measurements were made of energy-dependent quenching of atebrin fluorescence in membrane particles prepared from Escherichia coli grown anaerobically with glycerol as carbon source in the presence of either nitrate or fumarate. It is concluded that this technique can be used to study the functional organization of the anaerobic proton-translocating electron-transport chains that use nitrate or fumarate as terminal electron acceptor.

scholarly journals Effects of sulphate-limited growth in continuous culture on the electron-transport chain and energy conservation in Escherichia coli K12

1975 ◽  
Vol 152 (3) ◽  
pp. 537-546 ◽  
Author(s):  
R K Poole ◽  
B A Haddock
Keyword(s):  
Escherichia Coli ◽  
Electron Transport ◽  
Electron Transport Chain ◽  
Functional Organization ◽  
Extracellular Polysaccharide ◽  
Limited Growth ◽  
Escherichia Coli K12 ◽  
Transport Chain ◽  
Respiratory Chains ◽  
Energy Dependent

Growth of Escherichia coli K12 in a chemostat was limited by sulphate concentrations lower than 300 muM. The synthesis of extracellular polysaccharide and a change in morphology accompanied sulphate-limited growth. Growth yields with respect to the amount of glycerol or oxygen consumed were sixfold and twofold lower respectively under these conditions than when growth was limited by glycerol. Sulphate-limited cells lacked the proton-translocating oxidoreduction segment of the electron-transport chain between NADH and the cytochromes, and particles prepared from these cells lacked the energy-dependent reduction of NAD+ by succinate, DL-α-glycerophosphate or D-lactate, suggesting the loss of site-I phosphorylation. Glycerol-limited cells contained cytochrome b556, b562 and o, ubiquinone and low concentrations of menaquinone. Sulphate limitation resulted in the additional synthesis of cytochromes d, a1, b558 and c550; the amount of ubiquinone was decreased and menaquinone was barely detectable. Non-haem iron and acid-labile sulphide concentrations were twofold lower in electron-transport particles prepared from sulphate-limited cells. Recovery of site-I phosphorylation could not be demonstrated after incubating sulphate-limited cells with or without glycerol, in either the absence or presence of added sulphate. The loss of site-I phosphorylation in sulphate-limited cells is discussed with reference to the accompanying alterations in cytochrome composition of such cells. Schemes are proposed for the functional organization of the respiratory chains of E. coli grown under conditions of glycerol or sulphate limitation.

scholarly journals Escherichia coli cytochrome c peroxidase is a respiratory oxidase that enables the use of hydrogen peroxide as a terminal electron acceptor

2017 ◽  
Vol 114 (33) ◽  
pp. E6922-E6931 ◽  
Author(s):  
Maryam Khademian ◽  
James A. Imlay
Keyword(s):  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Carbon Source ◽  
Electron Acceptor ◽  
Electron Acceptors ◽  
Flux Rate ◽  
Terminal Electron Acceptor ◽  
E Coli ◽  
Nonfermentable Carbon Source ◽  
Quinone Pool

Microbial cytochrome c peroxidases (Ccp) have been studied for 75 years, but their physiological roles are unclear. Ccps are located in the periplasms of bacteria and the mitochondrial intermembrane spaces of fungi. In this study, Ccp is demonstrated to be a significant degrader of hydrogen peroxide in anoxic Escherichia coli. Intriguingly, ccp transcription requires both the presence of H2O2 and the absence of O2. Experiments show that Ccp lacks enough activity to shield the cytoplasm from exogenous H2O2. However, it receives electrons from the quinone pool, and its flux rate approximates flow to other anaerobic electron acceptors. Indeed, Ccp enabled E. coli to grow on a nonfermentable carbon source when H2O2 was supplied. Salmonella behaved similarly. This role rationalizes ccp repression in oxic environments. We speculate that micromolar H2O2 is created both biologically and abiotically at natural oxic/anoxic interfaces. The OxyR response appears to exploit this H2O2 as a terminal oxidant while simultaneously defending the cell against its toxicity.

scholarly journals Synthesis of alternative membrane-bound redox carriers during aerobic growth of Escherichia coli in the presence of potassium cyanide

1975 ◽  
Vol 148 (2) ◽  
pp. 349-352 ◽  
Author(s):  
J R Ashcroft ◽  
B A Haddock
Keyword(s):  
Escherichia Coli ◽  
Electron Transport ◽  
Carbon Source ◽  
Potassium Cyanide ◽  
Growth Conditions ◽  
Aerobic Growth ◽  
E Coli ◽  
Low Concentrations ◽  
Electron Transport Chains ◽  
Membrane Bound

Aerobic growth of Escherichia coli with an oxidizable substrate as carbon source in the presence of low concentrations of KCN leads to the synthesis and integration into the membrane of menaquinone and cytochromes b558, a1 and d in addition to the redox carriers normally present under aerobic growth conditions, namely ubiquinone and cytochromes b562, b556 and o. The results are discussed with reference to other phenotypic and genotypic modifications to the electron-transport chains of E. coli.

Effect of ascorbate on oxygen uptake and growth of Escherichia coli B

1988 ◽  
Vol 34 (6) ◽  
pp. 822-824 ◽  
Author(s):  
Holly E. Richter ◽  
Jacek Switala ◽  
Peter C. Loewen
Keyword(s):  
Escherichia Coli ◽  
Oxygen Uptake ◽  
Electron Acceptor ◽  
Minimal Medium ◽  
Anaerobic Growth ◽  
Rich Medium ◽  
Terminal Electron Acceptor ◽  
Subsequent Change ◽  
Escherichia Coli B

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.

Studies about the Mechanism of Herbicidal Interaction with Photosystem II in Isolated Chloroplasts

1979 ◽  
Vol 34 (11) ◽  
pp. 1010-1014 ◽  
Author(s):  
Gernot Renger
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Excitation Energy ◽  
Electron Acceptor ◽  
Functional Organization ◽  
Regulatory Element ◽  
Release Kinetics ◽  
Acceptor Side ◽  
Receptor Sites ◽  
Isolated Chloroplasts

Abstract Based on the functional organization scheme of system-II-electron transport and its modification by different procedures a proteinaceous component enwrapping the redox components (plastoquinone molecules) of the acceptor side (thereby acting as regulatory element) is inferred to be the unique target for herbicidal interaction with system II. This proteinaceous component, which is attacked by trypsin, provides the receptor sites for the herbicides. Studies of the release kinetics in trypsinated chloroplasts of the inhibition of oxygen evolution with K3 [Fe (CN)6] as electron acceptor indicates, that there exists a binding area with different specific subreceptor sites rather than a unique binding site for the various types of inhibitors. Furthermore, trypsination of the proteinaceous component enhances the efficiency of the plastoquinone pool to act as a non-photochemical quencher for excitation energy.

scholarly journals Lactobacillus plantarum WCFS1 Electron Transport Chains

2009 ◽  
Vol 75 (11) ◽  
pp. 3580-3585 ◽  
Author(s):  
R. J. W. Brooijmans ◽  
W. M. de Vos ◽  
J. Hugenholtz
Keyword(s):  
Electron Transport ◽  
Lactobacillus Plantarum ◽  
Consumption Rate ◽  
Growth Media ◽  
Terminal Electron Acceptor ◽  
Glucose Levels ◽  
Transport Chain ◽  
Electron Transport Chains ◽  
Cofactor Biosynthesis ◽  
Isogenic Mutants

ABSTRACT Lactobacillus plantarum WCFS1 requires both heme and menaquinone to induce respiration-like behavior under aerobic conditions. The addition of these compounds enhanced both biomass production, without progressive acidification, and the oxygen consumption rate. When both heme and menaquinone were present, L. plantarum WCFS1 was also able to reduce nitrate. The ability to reduce nitrate was severely inhibited by the glucose levels that are typically found in L. plantarum growth media (1 to 2% [vol/vol] glucose). In contrast, comparable mannitol levels did not inhibit the reduction of nitrate. L. plantarum reduced nitrate with concomitant formation of nitrite and ammonia. Genes that encode a bd-type cytochrome (cydABCD) and a nitrate reductase (narGHJI) were identified in the genome of L. plantarum. The narGHJI operon is part of a cluster of genes that includes the molybdopterin cofactor biosynthesis genes and narK. Besides a menaquinone source, isogenic mutants revealed that cydA and ndh1 are required for the aerobic-respiration-like response and narG for nitrate reduction. The ndh1 mutant was still able to reduce nitrate. The existence of a nonredundant branched electron transport chain in L. plantarum WCFS1 that is capable of using oxygen or nitrate as a terminal electron acceptor is proposed.

scholarly journals The fixA and fixB Genes Are Necessary for Anaerobic Carnitine Reduction in Escherichia coli

2002 ◽  
Vol 184 (14) ◽  
pp. 4044-4047 ◽  
Author(s):  
Angelique Walt ◽  
Michael L. Kahn
Keyword(s):  
Escherichia Coli ◽  
Electron Acceptor ◽  
Anaerobic Conditions ◽  
Terminal Electron Acceptor ◽  
E Coli ◽  
Carnitine Metabolism

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.

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