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Nitric oxide dioxygenase: an enzymic function for flavohemoglobin

P R Gardner1, A M Gardner, L A Martin

  • 1Division of Critical Care Medicine, Children's Hospital Medical Center, and Department of Pediatrics, University of Cincinnati, 3333 Burnet Avenue, Cincinnati, OH 45229, USA. gardp0@chmcc.org

Proceedings of the National Academy of Sciences of the United States of America
|September 2, 1998
PubMed
Summary
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Escherichia coli uses flavohemoglobin to detoxify nitric oxide (NO), converting it to nitrate. This discovery suggests NO detoxification is an ancient function of hemoglobins, predating oxygen transport.

Area of Science:

  • Microbiology
  • Biochemistry
  • Evolutionary Biology

Background:

  • Nitric oxide (NO) is a cellular toxin.
  • Organisms have evolved NO detoxification mechanisms.
  • Escherichia coli mutants resistant to NO were studied.

Purpose of the Study:

  • To identify the enzyme responsible for nitric oxide detoxification in Escherichia coli.
  • To elucidate the function of flavohemoglobin in NO metabolism.

Main Methods:

  • Isolation and characterization of NO-resistant mutants.
  • Reconstitution of NO-converting activity in cell extracts.
  • Genetic analysis using flavohemoglobin/NOD-deficient mutants.

Main Results:

Related Experiment Videos

  • NO-resistant mutants rapidly consumed NO.
  • A nitric oxide dioxygenase (NOD) activity was identified, requiring NADPH, FAD, and O2.
  • NOD activity was attributed to flavohemoglobin, which is inducible by NO.
  • Flavohemoglobin-deficient mutants showed sensitivity to NO.

    • Conclusions:

    • Escherichia coli flavohemoglobin functions as a nitric oxide dioxygenase (NOD).
    • NO detoxification is a primary role for flavohemoglobin.
    • This suggests that NO detoxification is an ancient hemoglobin function, potentially preceding oxygen transport.