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Nitric oxide as an antioxidant
Abstract
Benzoate monohydroxy compounds, and in particular salicylate, were produced during interaction of ferrous complexes with hydrogen peroxide (Fenton reaction) in a N2 environment. These reactions were inhibited when Fe complexes were flushed, prior to the addition in the model system, by nitric oxide. Methionine oxidation to ethylene by Fenton reagents was also inhibited by nitric oxide. Myoglobin in several forms such as metmyoglobin, oxymyoglobin, and nitric oxide-myoglobin were interacted with an equimolar concentration of hydrogen peroxide. Spectra changes in the visible region and the changes in membrane (microsomes) lipid peroxidation by the accumulation of thiobarbituric acid-reactive substances (TBA-RS) were determined. The results showed that metmyoglobin and oxymyoglobin were activated by H2O2 to ferryl myoglobin, which initiates membrane lipid peroxidation; but not nitric oxide-myoglobin, which, during interaction with H2O2, did not form ferryl but metmyoglobin which only poorly affected lipid peroxidation. It is assumed that nitric oxide, liganded to ferrous complexes, acts to prevent the prooxidative reaction of these complexes with H2O2.
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“The binding of NO to heme iron can also limit heme reactivity and prevent iron release from heme (482).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [482]
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Metadata
- Authors
- Kanner, J., Harel, S., & Rina, G.
- Affiliations
- Agricultural Research Organization (IL)
- Corresponding author
- Kanner, Joseph
- ORCID
- Kanner, Joseph
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1991-08
- Volume
- 289
- Issue
- 1
- Pages
- 130-136
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W1987165240
- Cited by
- 429
- References
- 47
- Citations by year
- 2025: 2 · 2024: 4 · 2023: 6 · 2022: 4 · 2021: 2 · 2020: 6 · 2019: 4 · 2018: 2 · 2017: 7 · 2016: 10 · 2015: 16 · 2014: 6 · 2013: 7 · 2012: 9
- FWCI
- 3.69
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- nitric oxide, antioxidant activity, Fenton reaction, hydrogen peroxide, iron(II) complexes, salicylates, methionine oxidation, myoglobin, metmyoglobin, oxymyoglobin, lipid peroxidation, microsomes, TBARS
- MeSH terms
- Antioxidants, Ascorbic Acid, Benzoates, Ferrous Compounds, Hydrogen Peroxide, Hydroxides, Hydroxylation, Methionine, Metmyoglobin, Myoglobin, Nitric Oxide, Salicylates, Ultraviolet Rays, Hydroxyl Radical, Benzoic Acid, Salicylic Acid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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