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Papers In Press, published online ahead of print December 18, 2001
J. Biol. Chem, 10.1074/jbc.M110470200
Submitted on October 31, 2001
Revised on December 11, 2001
Accepted on December 17, 2001

Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli: Evidence for a novel inducible anaerobic nitric oxide scavenging activity

Anne M. Gardner and Paul R. Gardner

Department of Critical Care Medicine, Children's Hospital Research Foundation, Cincinnati, OH 45229

Corresponding Author: gardp0{at}chmcc.org

Nitric oxide (NO) dioxygenase and NO reductase activities of flavohemoglobin (flavoHb) have been suggested as mechanisms for NO metabolism and detoxification in a variety of microbes. Mechanisms of NO detoxification were tested in Esherichia coli using flavoHb-deficient mutants and overexpressors. FlavoHb shows negligible anaerobic NO reductase activity and affords no protection to the NO-sensitive aconitase or the growth of anoxic E. coli, whereas the NO dioxygenase activity and the protection afforded with O2 are substantial. A NO-inducible, O2-sensitive, and cyanide-resistant NO reductase activity efficiently metabolizes NO and protects anaerobic cells from NO toxicity independent of the NO reductase activity of flavoHb. FlavoHb possesses nitrosoglutathione and nitrite reductase activities that may account for the protection it affords against these agents. NO detoxification by flavoHb occurs most effectively via O2-dependent NO dioxygenation.


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