Kinetic and Mechanistic Studies of the NO•-Mediated Oxidation of Oxymyoglobin and Oxyhemoglobin
Abstract
The second-order rate constants for the reactions between nitrogen monoxide and oxymyoglobin or oxyhemoglobin, determined by stopped-flow spectroscopy, increase with increasing pH. At pH 7.0 the rates are (43.6 +/- 0.5) x 10(6) M(-1) x s(-1) for oxymyoglobin and (89 +/- 3) x 10(6) M(-1) x s(-1) for oxyhemoglobin (per heme), whereas at pH 9.5 they are (97 +/- 3) x 10(6) M(-1) x s(-1) and (144 +/- 3) x 10(6) M(-1) x s(-1), respectively. The rate constants for the reaction between oxyhemoglobin and NO* depend neither on the association grade of the protein (dimer/tetramer) nor on the concentration of the phosphate buffer (100-1 mM). The nitrogen monoxide-mediated oxidations of oxymyoglobin and oxyhemoglobin proceed via intermediate peroxynitrito complexes which were characterized by rapid scan UV/vis spectroscopy. The two complexes MbFe(III)OONO and HbFe(III)OONO display very similar spectra with absorption maxima around 500 and 635 nm. These species can be observed at alkaline pH but rapidly decay to the met-form of the proteins under neutral or acidic conditions. The rate of decay of MbFe(III)OONO increases with decreasing pH and is significantly larger than those of the analogous complexes of the two subunits of hemoglobin. No free peroxynitrite is formed during these reactions, and nitrate is formed quantitatively, at both pH 7.0 and 9.0. This result indicates that, as confirmed from protein analysis after reacting the proteins with NO* for 10 times, when peroxynitrite is coordinated to the heme of myoglobin or hemoglobin it rapidly isomerizes to nitrate without nitrating the globins in physiologically significant amounts.
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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 [44]
Both ferrous deoxy and oxyheme react relatively rapidly with NO to produce nitrosyl heme or nitrate respectively.
“both ferrous deoxy and oxyheme react relatively rapidly (rate constants ~107 M-1s-1) with NO to produce nitrosyl heme (Scheme 1) or nitrate respectively [29, 30].”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [30]
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- Authors
- Herold, S., Exner, M., & Nauser, T.
- Affiliations
- ETH Zurich (CH)
- Corresponding author
- Herold, Susanna
- ORCID
- Nauser, Thomas
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-02-17
- Volume
- 40
- Issue
- 11
- Pages
- 3385-3395
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2011047569
- Cited by
- 324
- References
- 22
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 5 · 2023: 10 · 2022: 10 · 2021: 5 · 2020: 8 · 2019: 10 · 2018: 18 · 2017: 10 · 2016: 6 · 2015: 10 · 2014: 8 · 2013: 15 · 2012: 10
- FWCI
- 8.05
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Keywords
- nitric oxide, oxymyoglobin, oxyhemoglobin, peroxynitrite, heme oxidation, reaction kinetics, pH dependence, nitrate formation, metmyoglobin, methemoglobin, heme iron
- MeSH terms
- Animals, Chromatography, High Pressure Liquid, Horses, Humans, Hydrogen-Ion Concentration, Kinetics, Ligands, Metmyoglobin, Myoglobin, Nitrates, Nitric Oxide, Nitrogen Dioxide, Oxidation-Reduction, Oxyhemoglobins, Spectrophotometry, Ultraviolet, Spectrum Analysis
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