Glucose-dehydrogenase-mediated Solute Transport and ATP Synthesis in Acinetobacter calcoaceticus

Schie, B.J. Van; Pronk, Jack T.; Hellingwerf, K. J.; Dijken, J.P. Van; Kuenen, J.G.

doi:10.1099/00221287-133-12-3427

Cited by 11 publications

(13 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies on the generation of a proton motive force (Ap) by electron transfer in membrane vesicles of E. coli have shown that a significant decrease of Ap requires drastic inhibition of electron transfer (24). With D-lactate as the electron donor, the Ap remained essentially constant when the oxidation rate was inhibited up to 60%.…”

Section: Resultsmentioning

confidence: 99%

Inhibition of electron transfer and uncoupling effects by emodin and emodinanthrone in Escherichia coli

Ubbink-Kok¹,

Anderson²,

Konings³

1986

Antimicrob Agents Chemother

View full text Add to dashboard Cite

The anthraquinones emodin (1,3,8-trihydroxy-6-methylanthraquinone) and emodinanthrone (1,3,8-trihydroxy-6-methylanthrone) inhibited respiration-driven solute transport at micromolar concentrations in membrane vesicles of Escherichia coli. This inhibition was enhanced by Ca ions. The inhibitory action on solute transport'is caused by inhibition of electron flow in the respiratory chain, most likely at the level between ubiquinone and cytochrome b, and by dissipation of the proton motive force. The uncoupling action was confirmed by studies on the proton motive force in beef heart cytochrome oxidase proteoliposomes. Th"ese two effects on energy transduction in cytoplasmic membranes explain the antibiotic properties of emodin and emodinanthrone.Anthraquinones are produced by several organisms and especially by fungi (2). These compounds have been shown to exhibit a variety of biological effects like inhibition of growth of murine leukemia (15), mutagenicity (4), and h'epatotoxicity (17). These compounds have also been shown to be effective antibiotics at micromolar concentrations, especially for gram-positive bacteria (1,5,8).The anthraquinoid pigment emodin (1,3,8-trihydroxy-6-methylanthraquinone) is a metabolic product of Penicillium islandicum Sopp (9). Emodin was found to decrease the respiratory control index and P/O ratio in rat liver mitochondria markedly (16), indicating an uncoupling mode of action. A structural isomer of emodin, funiculosin, has been reported to be an effective inhibitor of the cytochrome bc1 segment in the respiratory chain of Saccharomyces cerevisiae (7) and rat liver mitochondria (22).Emodin and its precursor emodinanthrone (1,3,8-trihydroxy-6-methylanthrone) also possess antibiotic activity (8, 1), but the modes of action of these anthraquinones on bacterial cells have never been investigated. In view of the reports described above, a likely target for both compounds would be the energy-transducing properties of the cytoplasmic membrane.In this investigation, the effects of emodin and emodinanthrone on energy transduction in membrane vesicles of Escherichia coli were studied. The results demonstrated that both anthraquinone pigments inhibit electron flow in the respiratory chain and have uncoupling effects in this gram-negative bacterium.MATERIALS AND METHODS E. coli ML 308-225 (lacIP lacY+ lacZ-lacA-) was grown aerobically at 37°C on minimal medium A with 1% (wt/vol) sodium succinate and 0.1% (wt/vol) yeast extract. Logarithmically growing cells were harvested at an Aw of 0.8 to 1.Membrane vesicles were prepared as described by Kaback (12), suspended in 50 mM potassium phosphate (pH 7.0) at a protein concentration of approximately 10 mg/ml, and stored in liquid nitrogen.

show abstract

Section: Resultsmentioning

confidence: 99%

Inhibition of electron transfer and uncoupling effects by emodin and emodinanthrone in Escherichia coli

Ubbink-Kok¹,

Anderson²,

Konings³

1986

Antimicrob Agents Chemother

View full text Add to dashboard Cite

show abstract

“…Mitochondria and mitochondrial membranes of bovine heart (Smith, 1967) and N. crussu (Weiss et al, 1970), plasma membranes of E. coli strain B (Matsushita et al, 1987) and G. oxidans (van Schie et al, 1987), as well as complex I and the peripheral part of the complex both of N. crassa were prepared as described. The respiratory activities of isolated bovine heart and N. crussa mitochondria and plasma membranes from G. oxiduns were measured in a Clarke-type oxygen electrode (Weiss et al, 1970;Strohdeicher et al, 1990).…”

Section: Methodsmentioning

confidence: 99%

Two binding sites of inhibitors in NADH:ubiquinone oxidoreductase (complex I)

Friedrich

Heek

Leif

et al. 1994

European Journal of Biochemistry

247

157

View full text Add to dashboard Cite

The effect of ten naturally occurring and two synthetic inhibitors of NADH :ubiquinone oxidoreductase (complex I) of bovine heart, Neurosporu crassa and Escherichia coli and g1ucose:ubiquinone oxidoreductase (glucose dehydrogenase) of Gluconobacter oxidans was investigated. These inhibitors could be divided into two classes with regard to their specifity and mode of action. Class I inhibitors, including the naturally occuring piericidin A, annonin VI, phenalamid A2, aurachins A and B, thiangazole and the synthetic fenpyroximate, inhibit complex I from all three species in a partially competitive manner and glucose dehydrogenase in a competitive manner, both with regard to ubiquinone. Class I1 inhibitors including the naturally occuring rotenone, phenoxan, aureothin and the synthetic benzimidazole inhibit complex I from all species in an non-competitive manner, but have no effect on the glucose dehydrogenase. Myxalamid PI could not be classified as above because it inhibits only the mitochondrial complex I and in a competitive manner. All inhibitors affect the electron-transfer step from the high-potential iron-sulphur cluster to ubiquinone. Class I inhibitors appear to act directly at the ubiquinone-catalytic site which is related in complex I and glucose dehydrogenase.NADH : ubiquinone oxidoreductase, also known as respiratory complex I of mitochondria, transfers electrons from NADH to ubiquinone and links this process with translocation of protons across the inner membrane.

show abstract

“…The aerobic respiratory chain of E. coli is relatively simple, with respect to its components and its sequence, and has a number of primary dehydrogenases coupled to the respiratory chain, including flavoproteins such as D-lactate, succinate, and NADH dehydrogenases (13) and the quinoprotein GDH (25). The E. coli aerobic respiratory chain is also branched at the end with cytochrome o and cytochrome d as terminal oxidases.…”

mentioning

confidence: 99%

“…1), implying that GDH is rate limiting in the D-glucose oxidation. van Schie et al (25) showed that D-glucose oxidation generated A4i in E. coli membrane vesicles by using a tetraphenylphosphonium-electrode. Generation of A* was confirmed here by fluorescence quenching of diS-C3-(5) in RSO membrane vesicles of E. coli GR19N (Fig.…”

mentioning

confidence: 99%

Reconstitution of pyrroloquinoline quinone-dependent D-glucose oxidase respiratory chain of Escherichia coli with cytochrome o oxidase

Matsushita¹,

Nonobe²,

Shinagawa³

et al. 1987

J Bacteriol

View full text Add to dashboard Cite

D-Glucose dehydrogenase is a pyrroloquinoline quinone-dependent primary dehydrogenase linked to the respiratory chain of a wide variety of bacteria. The enzyme exists in the membranes of Escherichia coli, mainly as an apoenzyme which can be activated by the addition of pyrroloquinoline quinone and magnesium. Thus, membrane vesicles of E. coli can oxidize D-glucose to gluconate and generate an electrochemical proton gradient in the presence of pyrroloquinoline quinone. The D-glucose oxidase-respiratory chain was reconstituted into proteoliposomes, which consisted of two proteins purified from E. coli membranes, D-glucose dehydrogenase and cytochrome o oxidase, and E. coli phospholipids containing ubiquinone 8. The electron transfer rate during D-glucose oxidation and the membrane potential generation in the reconstituted proteoliposomes were almost the same as those observed in the membrane vesicles when pyrroloquinoline quinone was added. The results demonstrate that the quinoprotein, D-glucose dehydrogenase, can reduce ubiquinone 8 directly within phospholipid bilayer and that the D-glucose oxidase system of E. coli has a relatively simple respiratory chain consisting of primary dehydrogenase, ubiquinone 8, and a terminal oxidase.

show abstract

Glucose-dehydrogenase-mediated Solute Transport and ATP Synthesis in Acinetobacter calcoaceticus

Cited by 11 publications

References 18 publications

Inhibition of electron transfer and uncoupling effects by emodin and emodinanthrone in Escherichia coli

Inhibition of electron transfer and uncoupling effects by emodin and emodinanthrone in Escherichia coli

Two binding sites of inhibitors in NADH:ubiquinone oxidoreductase (complex I)

Reconstitution of pyrroloquinoline quinone-dependent D-glucose oxidase respiratory chain of Escherichia coli with cytochrome o oxidase

Contact Info

Product

Resources

About