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Related Experiment Videos

O2-dependent nitrogenase switch-off in Rhodobacter capsulatus E1F1.

C Moreno-Vivián1, F Castillo

  • 1Departamento de Bioquímica y Biología Molecular y Fisiología, Facultad de Ciencias, Universidad de Córdoba.

Microbiologia (Madrid, Spain)
|June 1, 1987
PubMed
Summary

Rhodobacter capsulatus E1F1 nitrogenase shows partial oxygen resistance. A protective system involving uptake hydrogenase and an inducible electron transport system helps shield nitrogenase from oxygen damage.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Enzymology

Background:

  • Nitrogenase is crucial for nitrogen fixation but sensitive to oxygen.
  • Understanding oxygen protection mechanisms in nitrogen-fixing bacteria is vital.

Purpose of the Study:

  • To investigate the oxygen resistance of nitrogenase in Rhodobacter capsulatus E1F1.
  • To elucidate the protective mechanisms against oxygen inactivation.

Main Methods:

  • Studying nitrogenase activity in Rhodobacter capsulatus E1F1 under varying oxygen conditions.
  • Assessing the effect of hydrogen and preincubation on oxygen inactivation.
  • Analyzing oxygen uptake rates in illuminated cells.

Main Results:

  • Nitrogenase of R. capsulatus E1F1 exhibited partial resistance to oxygen inactivation in vivo.

Related Experiment Videos

  • Inactivation was reversible under anaerobic conditions and independent of new protein synthesis.
  • Preincubation with low oxygen pressures or hydrogen reduced inactivation extent.
  • Oxygen uptake was enhanced by hydrogen, especially after oxygen preincubation.

    • Conclusions:

    • R. capsulatus E1F1 possesses an oxygen protective system for nitrogenase.
    • This system includes an uptake hydrogenase and an inducible electron transport system linked to the respiratory chain.