Cited by 139Hemoglobin structure and functionMetal-Catalyzed Oxygenation MechanismsProtein Interaction Studies and Fluorescence Analysis

Stoichiometry of the reaction of oxyhemoglobin with nitrite

Kosaka, Hiroaki, Imaizumi, Kazuhiko, Imai, Kiyohiro, Tyuma, Itiro·1979·Biochimica et Biophysica Acta (BBA) - Protein Structure

Abstract

During the reaction of oxyhemoglobin (HbO2) with nitrite, the concentration of residual nitrite, nitrate, oxygen, and methemoglobin (Hb+) was determined successively. The results obtained at various pH values indicate the following stoichiometry for the overall reaction: 4HbO2 + 4NO2- 4H+ leads to 4Hb+ + 4NO3- + O2 + 2H2 O (Hb denotes hemoglobin monomer). NO2- binds with methemoglobin noncooperatively with a binding constant of 340 M-1 at pH 7.4 and 25 degrees C. Thus, the major part of Hb+ produced is aquomethemoglobin, not methemoglobin nitrite, when less than 2 equivalents of nitrite is used for the oxidation.

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Crossref · 10.1016/0005-2795(79)90235-6

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Authors
Kosaka, H., Imaizumi, K., Imai, K., & Tyuma, I.
Affiliations
The University of Osaka (JP)
Venue
Biochimica et Biophysica Acta (BBA) - Protein Structure
Publisher
Elsevier BV
Published
1979-11
Volume
581
Issue
1
Pages
184-188
ISSN
0005-2795 (ISSN-L)
OpenAlex
W2077180688
Cited by
139
References
5
Citations by year
2024: 1 · 2022: 1 · 2020: 1 · 2018: 4 · 2017: 2 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 4 · 2012: 3
FWCI
3.30
Type
journal article
Language
en
Open access
closed
Locations
  • Biochimica et Biophysica Acta (BBA) - Protein Structure (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
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords
oxyhemoglobin, nitrite, methemoglobin, hemoglobin oxidation, reaction stoichiometry, non-cooperative binding, pH dependence, nitrate
MeSH terms
Hemoglobin A, Humans, Hydrogen-Ion Concentration, Kinetics, Methemoglobin, Nitrites, Oxyhemoglobins

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