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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.
Flavohemoglobin Detoxifies Nitric Oxide in Aerobic, but Not
Anaerobic, Escherichia coli
EVIDENCE FOR A NOVEL INDUCIBLE ANAEROBIC NITRIC OXIDE-SCAVENGING
ACTIVITY*
*
This work was supported in part by a grant from the
Children's Hospital Research Foundation Trustees, American Heart
Association Grant 9730193N, and National Institutes of Health Grant
GM65090.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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