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Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins
Abstract
Nitric oxide is unique among the higher oxides of nitrogen in its reactivity and efficiency for the oxidation of oxygen-bound hemoproteins. Dinitrogen trioxide serves as a nitric oxide donor, but dinitrogen tetroxide does not exhibit similar reactivity. Details are provided of the stoichiometric transformation through which nitric oxide is converted to nitrate with accompanying oxidation of myoglobin or hemoglobin to the corresponding iron(III) hemoprotein, including an estimate of the rate constant for nitric oxide oxidation of oxygen-associated myoglobin and the effect of unassociated oxygen on the stoichiometry and rates for nitric oxide oxidation. Evidence is presented to establish the mechanism of oxidation in the direct combination of nitric oxide with iron(II)-bound dioxygen.
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“The biggest conceptual challenge to the notion that deoxyHb plays a major role in bioactivation of nitrite is that NO produced in the red blood cell would be rapidly scavenged by the dioxygenation reaction where NO reacts with oxygenated Hb (OxyHb) to form MetHb and nitrate,”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [42]
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Metadata
- Authors
- Doyle, M. P., & Hoekstra, J. W.
- Affiliations
- Hope College (US)
- Corresponding author
- Doyle, Michael P.
- ORCID
- Doyle, Michael P.
- Venue
- Journal of Inorganic Biochemistry
- Publisher
- Elsevier BV
- Published
- 1981-01
- Volume
- 14
- Issue
- 4
- Pages
- 351-358
- ISSN
- 0162-0134 (ISSN-L)
- OpenAlex
- W2019435702
- Cited by
- 643
- References
- 24
- Citations by year
- 2026: 1 · 2025: 11 · 2024: 12 · 2023: 13 · 2022: 11 · 2021: 13 · 2020: 14 · 2019: 14 · 2018: 19 · 2017: 12 · 2016: 7 · 2015: 17 · 2014: 13 · 2013: 26 · 2012: 15
- FWCI
- 1.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Inorganic Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- NO oxidation, heme proteins, myoglobin, hemoglobin, dinitrogen trioxide, dinitrogen tetroxide, nitrate formation, reaction mechanism, rate constants
- MeSH terms
- Animals, Hemoglobin A, Horses, Humans, Kinetics, Myocardium, Myoglobin, Nitric Oxide, Nitrogen Oxides, Oxidation-Reduction, Oxyhemoglobins
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.
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