Cited by 643Hemoglobin structure and functionMetal-Catalyzed Oxygenation MechanismsNitric Oxide and Endothelin Effects

Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins

Doyle, Michael P., Hoekstra, James W.·1981·Journal of Inorganic Biochemistry

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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Crossref · 10.1016/s0162-0134(00)80291-3

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24 of 24 references verified0 citation errors · 0 not checkable

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  • NO produced in the red blood cell would be rapidly scavenged by the dioxygenation reaction where NO reacts with oxygenated Hb to form MetHb and nitrate.

    “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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Authors
Doyle, M. P., & Hoekstra, J. W.
Affiliations
Hope College (US)
Corresponding author
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 › Cell Biology › Hemoglobin structure and function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Health Sciences › Medicine › Physiology › 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

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