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J. Biol. Chem., Vol. 277, Issue 10, 8166-8171, March 8, 2002
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From the Division of Critical Care Medicine, Children's Hospital
Medical Center, Cincinnati, Ohio 45229
Nitric-oxide dioxygenase (NOD) and reductase
(NOR) 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
Escherichia coli using flavoHb-deficient mutants and
overexpressors. flavoHb showed negligible anaerobic NOR activity and
afforded no protection to the NO-sensitive aconitase or the growth of
anoxic E. coli, whereas the NOD activity and the protection
afforded with O2 were substantial. A NO-inducible,
O2-sensitive, and cyanide-resistant NOR activity efficiently metabolized NO and protected anaerobic cells from NO
toxicity independent of the NOR 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.
To whom correspondence should be addressed: Div. of Critical Care
Medicine, MLC7006, Children's Hospital Medical Center, 3333 Burnet
Ave., Cincinnati, OH 45229. Tel.: 513-636-4885; Fax: 513-636-4892; E-mail: gardp0@chmcc.org.
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