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

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Stoichiometry of the reaction of oxyhemoglobin with nitrite

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

DOI 10.1016/0005-2795(79)90235-6

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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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Authors: Kosaka, H., Imaizumi, K., Imai, K., & Tyuma, I.
Affiliations: The University of Osaka (JP)
ORCID: Imaizumi, Kazuhiko
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)
DOI: 10.1016/0005-2795(79)90235-6
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochimica et Biophysica Acta (BBA) - Protein Structure (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
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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Stoichiometry of the reaction of oxyhemoglobin with nitrite

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