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Related Experiment Videos

Membrane-associated chromate reductase activity from Enterobacter cloacae.

P C Wang1, T Mori, K Toda

  • 1Institute of Applied Microbiology, University of Tokyo, Japan.

Journal of Bacteriology
|March 1, 1990
PubMed
Summary

Enterobacter cloacae HO1 anaerobically reduces toxic hexavalent chromium. This chromate reductase activity is primarily located in the cell membrane fraction, especially in membrane vesicles.

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Area of Science:

  • Environmental Microbiology
  • Biochemistry
  • Toxicology

Background:

  • Hexavalent chromium (Cr(VI)) is a toxic environmental pollutant.
  • Microbial reduction of Cr(VI) is a key detoxification pathway.

Purpose of the Study:

  • To investigate the anaerobic reduction of hexavalent chromium by Enterobacter cloacae HO1.
  • To identify the cellular location of chromate reductase activity.

Main Methods:

  • Anaerobic culture of Enterobacter cloacae HO1.
  • Cell fractionation to isolate membrane components.
  • Assay of chromate reductase activity in membrane vesicles using electron donors.

Main Results:

  • Enterobacter cloacae HO1 cells reduced hexavalent chromium under anaerobic conditions.

Related Experiment Videos

  • Chromate reductase activity was predominantly found in the cell membrane fraction.
  • Right-side-out membrane vesicles exhibited significant chromate reductase activity with ascorbate-reduced phenazine methosulfate.

    • Conclusions:

    • The cell membrane of Enterobacter cloacae HO1 harbors the primary chromate reductase activity.
    • Membrane vesicles are suitable for studying this enzyme's function in hexavalent chromium detoxification.