Purification and properties of glucose dehydrogenase and cytochrome b from Bacterium anitratum

Hauge, Jens G.

doi:10.1016/0006-3002(60)91449-9

Cited by 54 publications

(26 citation statements)

References 19 publications

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“…Electron transport from GDH proceeds via cytochrome b (Hauge, 1960;Beardmore-Gray & Anthony, 1986). In A. calcoaceticus terminal oxidation may proceed via cytochrome o or cytochrome d. The level of these cytochromes in the membrane is dependent upon the O2 concentration in the growth medium (Ensley & Finnerty, 1980).…”

Section: Discussionmentioning

confidence: 99%

“…The characteristics of GDH from 'Bacterium anitraturn' (Acinetobucter calcoaceticus) were extensively studied by Hauge (1960). The nature of the unusual cofactor of the enzyme was, however, established only recently : the enzyme belongs to the class of quinoproteins which have pyrrolo-quinoline quinone (PQQ) as the prosthetic group .…”

Section: Introductionmentioning

confidence: 99%

“…The nature of the unusual cofactor of the enzyme was, however, established only recently : the enzyme belongs to the class of quinoproteins which have pyrrolo-quinoline quinone (PQQ) as the prosthetic group . GDH is coupled to the electron transport chain at the level of cytochrome b (Hauge, 1960;Beardmore-Gray & Anthony, 1986).…”

Section: Introductionmentioning

confidence: 99%

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

Schie¹,

Pronk²,

Hellingwerf³

et al. 1987

Microbiology

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Evidence is presented that in Acinetobacter calcoaceticus oxidation of glucose to gluconate by the periplasmic quinoprotein glucose dehydrogenase (EC 1 . 1 .99.17) leads to energy conservation.Membrane vesicles prepared from cells grown in carbon-limited chemostat culture exhibited (1) a high rate of glucose-dependent oxygen consumption and gluconate production, (2) glucosemediated cytochrome reduction, (3) uncoupler sensitive, glucose-dependent generation of a membrane potential and (4) glucose-driven accumulation of amino acids. Furthermore, oxidation of glucose to gluconate by whole cells was associated with ATP synthesis. These results confirm and extend previous observations that periplasmic glucose oxidation can act as a driving force for energy-requiring processes. It is therefore concluded that the incomplete oxidation of glucose by bacteria may serve as an auxiliary energy-generating system.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Schie¹,

Pronk²,

Hellingwerf³

et al. 1987

Microbiology

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“…The enzyme was found to contain an unknown cofactor (Hauge 1960), later identified as PQQ . A detailed characterization of this enzyme from A. calcoaceticus showed that glucose dehydrogenase is a membrane-bound periplasmic enzyme, containing two molecules of PQQ per enzyme molecule (Dokter et al 1986).…”

Section: Introductionmentioning

confidence: 99%

Effects of growth rate and oxygen tension on glucose dehydrogenase activity inAcinetobacter calcoaceticus LMD 79.41

Schie

Dijken

Kuenen

1989

Antonie van Leeuwenhoek

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The regulation of the synthesis of the quinoprotein glucose dehydrogenase (EC 1.1.99.17) has been studied in Acinetobacter calcoaceticus LMD 79.41, an organism able to oxidize glucose to gluconic acid, but unable to grow on both compounds. Glucose dehydrogenase was synthesized constitutively in both batch and carbon-limited chemostat cultures on a variety of substrates. In acetate-limited chemostat cultures glucose dehydrogenase levels and the glucose-oxidizing capacity of whole cells were dependent on the growth rate. They strongly increased at low growth rates at which the maintenance requirement of the cells had a pronounced effect on biomass yield. Cultures grown on a mixture of acetate and glucose in carbon and energy-limited chemostat cultures oxidized glucose quantitatively to gluconic acid. However, during oxygen-limited growth on this mixture glucose was not oxidized and only very low levels of glucose dehydrogenase were detected in cell-free extracts. After introduction of excess oxygen, however, cultures or washed cell suspensions almost instantaneously gained the capacity to oxidize glucose at a high rate, by an as yet unknown mechanism.

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“…calcoaceticus is kinetically distinct from the 'NADH oxidase' system, although both the GDH and the NADH de hydrogenase were assumed to donate electrons via ubiquinone-9, the b-type cytochromes and the cytochrome o-type oxidase to oxygen. In contrast to this direct electron transfer to ubiquinone, for the soluble GDH it has been suggested that the soluble cytochrome b-562 functions between the GDH and ubiquinone (Hauge, 1960(Hauge, , 1961Dokter et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Purification and partial characterization of the membrane-bound haem-containing proteins from Acinetobacter calcoaceticus LMD 79.41

Dokter

Wielink

Geerlof

et al. 1990

Journal of General Microbiology

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Cytoplasmic membranes of Acinetobucter cdcoaceticus cells, cultured under acetate-limiting conditions, contain cytochrome bSs4 and a cytochrome o-containing oxidase. Both have been purified to homogeneity and characterized. Cytochrome bss4 is a monomeric protein (molecular mass 70 kDa) with a midpoint potential of + lo0 mV (in the membrane it has most probably a value of +50 mV). The cytochrome o-containing oxidase seems to be an aPy8 protein since the molecular mass of the native protein was estimated to be 150 kDa and the molecular masses of the subunits, determined by SDS-polyacrylamide-gel electrophoresis, are 55, 41, 33 and 17 kDa. Redox spectroscopy of the purified complex shows the presence of a cytochrome bss5,563 having a midpoint potential of approximately + 160 mV (both in purified form and in the membrane). CO difierence spectroscopy shows the presence of a second b-type cytochrome, viz. cytochrome 0. Cytoplasmic membranes of A. calcoaceticus cells grown under oxygen-limiting conditions also show the presence of the cytochrome bSs4 and the cytochrome o-containing oxidase. In addition a protein has been solubilized with the spectral characteristics of a cytmhrome d-containing oxidase. The cytochrome o-and d-containing oxidases appear to be similar to those reported for Esckrichia coli and Profeus mirabilis. On the other hand, cytochrome bSs4 has no counterpart in these organisms since the cytochrome bSs6 described for E. cofi is quite dissimilar.

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Purification and properties of glucose dehydrogenase and cytochrome b from Bacterium anitratum

Cited by 54 publications

References 19 publications

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

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

Effects of growth rate and oxygen tension on glucose dehydrogenase activity inAcinetobacter calcoaceticus LMD 79.41

Purification and partial characterization of the membrane-bound haem-containing proteins from Acinetobacter calcoaceticus LMD 79.41

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