โ Scribed by R. W. J. Hommes; B. Hell; P. W. Postma; O. M. Neijssel; D. W. Tempest
No coin nor oath required. For personal study only.
In order to assess the functional significance of the quinoprotein glucose dehydrogenase recently found to be present in K+-limited Klebsiella aerogenes, a broad study was made of the influence of specific environmental conditions on the cellular content of this enzyme. Whereas high activities were manifest in cells from glucose containing chemostat cultures that were either potassium-or phosphate-limited, only low activities were apparent in cells from similar cultures that were either glucose-, sulphate-or ammonia-limited. With these latter two cultures, a marked increase in glucose dehydrogenase activity was observed when 2,4-dinitrophenol (1 mM end concentration) was added to the growth medium. These results suggested that the synthesis of glucose dehydrogenase is not regulated by the level of glucose in the growth medium, but possibly by conditions that imposed an energetic stress upon the cells. This conclusion was further supported by a subsequent finding that K +-limited cells that were growing on glycerol also synthesized substantial amounts of glucose dehydrogenase.
The enzyme was found to be membrane associated, and preliminary evidence has been obtained that it is located on the periplasmic side of the cytoplasmic membrane and functionally linked to the respiratory chain. This structural and functional orientation is consistent with glucose dehydrogenase serving as a low impedance energy generating system.
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No holoenzyme pyrroloquinoline quinone (PQQ)dependent glucose dehydrogenase and only very low apoenzyme levels could be detected in cells of Klebsiella pneumoniae, growing anaerobically, or carrying out a fumarate or nitrate respiration. Low glucose dehydrogenase activity in some aerobic glucose-exc
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