The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Nitrosative stress: Metabolic pathway involving the flavohemoglobin
Open accessAbstract
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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“Higher concentrations of NO (>1 μM) can lead not only to oxidative stress but also nitrative and nitrosative stress via the generation of peroxynitrite and nitrosating species”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [411]
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Cites
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Self-citationRedox signaling: Nitrosylation and related target interactions of nitric oxide
Stamler, J. S. (1994) · Cell · doi:10.1016/0092-8674(94)90269-0 · Cited by 1,723
Self-citationS-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
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Self-citationSuperoxide Anion Radical (O·̄2), Superoxide Dismutases, and Related Matters
Fridovich, I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18515 · Cited by 1,337
Fang, F. C. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119473 · Cited by 1,139
Activation of the Cardiac Calcium Release Channel (Ryanodine Receptor) by Poly-S-Nitrosylation
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Self-citation(S)NO Signals: Translocation, Regulation, and a Consensus Motif
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Self-citationReactions between nitric oxide and haemoglobin under physiological conditions
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Self-citationGlutathione Peroxidase Protects against Peroxynitrite-mediated Oxidations
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Metadata
- Authors
- Hausladen, A., Gow, A. J., & Stamler, J. S.
- Affiliations
- Howard Hughes Medical Institute (US)
- 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
- 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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