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Cited by 175

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Flavohemoglobin Detoxifies Nitric Oxide in Aerobic, but Not Anaerobic, Escherichia coli

Open access
Gardner, Anne M., Gardner, Paul R.·2002·Journal of Biological Chemistry

Abstract

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 O(2) were substantial. A NO-inducible, O(2)-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 O(2)-dependent NO dioxygenation.

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Metadata

Authors
Gardner, A. M., & Gardner, P. R.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-03
Volume
277
Issue
10
Pages
8166-8171
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2003811454
Cited by
175
References
3
FWCI
3.54
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Flavohemoglobin Detoxifies Nitric Oxide in Aerobic, but Not Anaerobic, Escherichia coli. https://app.cochat.ai/papers/10.1074/jbc.m110470200
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Gardner, A. M., & Gardner, P. R. (2002). Flavohemoglobin Detoxifies Nitric Oxide in Aerobic, but Not Anaerobic, Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m110470200

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