Archives of Microbiology

, Volume 116, Issue 3, pp 221–229 | Cite as

Physiological characterization of the hydrogen bacterium Aquaspirillum autotrophicum

  • M. Aragno
  • H. G. Schlegel


Aquaspirillum autrotrophicum, an aerobic hydrogen bacterium recently isolated from an eutrophic freshwater lake, was characterized physiologically. It grew autotrophically in a fermenter with a doubling time of 4 h. Heterotrophic growth was faster. pH-Optimum ranged from 5.0–7.5, temperature optimum was about 28° C. During autotrophic growth about 10 moles hydrogen were consumed per 1 mole carbon dioxide fixed.

Hydrogenase activity is inducible. CO2 did not enhance the oxy-hydrogen reaction by intact cells. The hydrogenase activity was localized in the particulate fraction. The hydrogenase reduced methylene blue and phenazine methosulfate; pyridine nucleotides were not reduced. In cell-free extracts, hydrogenase was sensitive to oxygen. Ribulosebisphosphate carboxylase was present in autotrophically-grown cells and absent from heterotrophically grown cells.

Hydrogenase induction in heterotrophically-grown cells followed parabolic kinetics. Oxygen and D-gluconate repressed hydrogenase synthesis, whereas citrate, DL-lactate and pyruvate stimulated its formation. The repressive effect was delayed. The results suggest that the control of hydrogenase synthesis occurred at the transcriptional level, and that mRNA coding for the hydrogenase had a relatively long life span.

D-Gluconate was degraded via the Entner-Doudoroff pathway, the enzymes of which were constitutively formed. Enzymes of the pentosephosphate and Embden-Meyerhof pathways (except phosphofructokinase) were present, too. Hydrogen did not inhibit heterotrophic growth.

The possible competitive advantage of the physiological properties described with regard to the natural habitat was discussed.

Key words

Aquaspirillum autotrophicum Hydrogen bacterium Growth Chemolithoautotrophy Particulate hydrogenase Induction Repression Natural habitats 

Non-Standard Abbreviations




glyceraldehyde-3-phosphate dehydrogenase


optical density




triosephosphate isomerase


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Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • M. Aragno
    • 1
    • 2
    • 3
  • H. G. Schlegel
    • 1
    • 2
    • 3
  1. 1.Institut für Mikrobiologie der Universität GöttingenMünchen, in GöttingenGermany
  2. 2.Gesellschaft für Strahlen- und Umweltforschung mbHMünchen, in GöttingenGermany
  3. 3.Laboratoire de Microbiologie de l'Institut de BotaniqueUniversité de NeuchâtelNeuchâtlSwitzerland

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