Cited by 285Hemoglobin structure and functionNitric Oxide and Endothelin EffectsHeme Oxygenase-1 and Carbon Monoxide

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Nitrosative stress: Metabolic pathway involving the flavohemoglobin

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Hausladen, Alfred, Gow, Andrew J., Stamler, Jonathan S.·1998·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.95.24.14100PMC PMC24333

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Abstract

Nitric oxide (NO) biology has focused on the tightly regulated enzymatic mechanism that transforms l -arginine into a family of molecules, which serve both signaling and defense functions. However, very little is known of the pathways that metabolize these molecules or turn off the signals. The paradigm is well exemplified in bacteria where S -nitrosothiols (SNO)—compounds identified with antimicrobial activities of NO synthase—elicit responses that mediate bacterial resistance by unknown mechanisms. Here we show that Escherichia coli possess both constitutive and inducible elements for SNO metabolism. Constitutive enzyme(s) cleave SNO to NO whereas bacterial hemoglobin, a widely distributed flavohemoglobin of poorly understood function, is central to the inducible response. Remarkably, the protein has evolved a novel heme-detoxification mechanism for NO. Specifically, the heme serves a dioxygenase function that produces mainly nitrate. These studies thus provide new insights into SNO and NO metabolism and identify enzymes with reactions that were thought to occur only by chemical means. Our results also emphasize that the reactions of SNO and NO with hemoglobins are evolutionary conserved, but have been adapted for cell-specific function.

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Authors: Hausladen, A., Gow, A. J., & Stamler, J. S.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Hausladen, Alfred
Gow, Andrew J.
Stamler, Jonathan S.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1998-11-24
Volume: 95
Issue: 24
Pages: 14100-14105
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.95.24.14100
PMC: PMC24333
OpenAlex: W2069848230
Cited by: 285
References: 37
Citations by year: 2026: 2 · 2025: 3 · 2024: 2 · 2022: 7 · 2021: 5 · 2020: 8 · 2019: 8 · 2018: 7 · 2017: 2 · 2016: 7 · 2015: 4 · 2014: 10 · 2013: 13 · 2012: 17
FWCI: 5.88
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01hl052529-05)
National Heart, Lung, and Blood Institute (HL 52529, R01HL059130, HL 59130)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
Keywords: nitrosative stress, flavohemoglobin, nitric oxide metabolism, S-nitrosothiols, Escherichia coli, nitrate formation, bacterial hemoglobin, nitric oxide detoxification
MeSH terms: Cysteine, Diethylamines, Enzyme Inhibitors, Escherichia coli, Biological Evolution, Heme, Hemeproteins, Kinetics, Nitric Oxide, Nitrogen Oxides, Nitroso Compounds, Spectrophotometry, Tryptophan Oxygenase, Signal Transduction, S-Nitrosothiols

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Nitrosative stress: Metabolic pathway involving the flavohemoglobin

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