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Cited by 55Hemoglobin structure and functionMetal-Catalyzed Oxygenation MechanismsNitric Oxide and Endothelin Effects

Mechanistic Studies of the Oxidation of Oxyhemoglobin by Peroxynitrite

Boccini, Francesca, Herold, Susanna·2004·Biochemistry
DOI 10.1021/bi0482250
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Abstract

The strong oxidizing and nitrating agent peroxynitrite has been shown to diffuse into erythrocytes and oxidize oxyhemoglobin (oxyHb) to metHb. Because the value of the second-order rate constant for this reaction is on the order of 10(4) M(-)(1) s(-)(1) and the oxyHb concentration is about 20 mM (expressed per heme), this process is rather fast and oxyHb is considered a sink for peroxynitrite. In this work, we showed that the reaction of oxyHb with peroxynitrite, both in the presence and absence of CO(2), proceeds via the formation of oxoiron(iv)hemoglobin (ferrylHb), which in a second step is reduced to metHb and nitrate by its reaction with NO(2)(*). In the presence of physiological relevant amounts of CO(2), ferrylHb is generated by the reaction of NO(2)(*) with the coordinated superoxide of oxyHb (HbFe(III)O(2)(*)(-)). This reaction proceeds via formation of a peroxynitrato-metHb complex (HbFe(III)OONO(2)), which decomposes to generate the one-electron oxidized form of ferrylHb, the oxoiron(iv) form of hemoglobin with a radical localized on the globin. CO(3)(*)(-), the second radical formed from the reaction of peroxynitrite with CO(2), is also scavenged efficiently by oxyHb, in a reaction that finally leads to metHb production. Taken together, our results indicate that oxyHb not only scavenges peroxynitrite but also the radicals produced by its decomposition.

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  • In the cardiovascular system, peroxynitrite can oxidize heme proteins, such as Hb and Mb, resulting in the oxidation of their heme oxygen-carrying site from ferrous iron to ferric heme.

    “In the cardiovascular system, peroxynitrite can oxidize heme proteins, such as Hb and Mb, resulting in the oxidation of their heme oxygen–carrying site from ferrous iron to ferric heme (101, 942).”

    From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [101]

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Authors
Boccini, F., & Herold, S.
Affiliations
ETH Zurich (CH)
Corresponding author
Herold, Susanna
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2004-12-01
Volume
43
Issue
51
Pages
16393-16404
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi0482250
OpenAlex
W1984430138
Cited by
55
References
26
Citations by year
2026: 2 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 2 · 2015: 2 · 2014: 3 · 2013: 2
FWCI
2.45
Type
journal article
Language
en
Open access
closed
Locations
  • 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
peroxynitrite, oxyhemoglobin, nitrite, superoxide, carbon dioxide, free radical scavenging, reaction mechanism, erythrocytes, hemoglobin oxidation
MeSH terms
Carbon Dioxide, Humans, Hydrogen-Ion Concentration, Kinetics, Methemoglobin, Oxidation-Reduction, Oxyhemoglobins, Spectrophotometry, Ultraviolet, Time Factors, Peroxynitrous Acid

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