Nitrite catalyzes ferriheme protein reductive nitrosylation
Abstract
Nitrite ion is found to catalyze the NO reduction of met-hemoglobin and met-myoglobin in pH 7.0 buffered aqueous solution. The catalysis rate constants for these ferriheme proteins and for two water-soluble ferriheme model systems follow the same order as do the FeIII/II reduction potentials of the ferric nitrosyl complexes. This is consistent with a proposed mechanism occurring via outer sphere reduction of the FeIII(NO) center by NO2- to give the FeII(NO) product plus NO2. Although the first step is thermodynamically uphill, the NO2 generated would be rapidly trapped by excess NO to form N2O3, which would hydrolyze. We speculate that, if formed in the proximity of the protein, the strong nitrosating agent N2O3 could also result in protein modifications.
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Recent evidence points to dinitrogen trioxide (N2O3) as a plausible intermediate for generation of NO downstream from nitrite reduction.
“Recent evidence points towards the formation of the nitrosating agent dinitrogen trioxide (N2O3) as one such plausible intermediate for the generation of NO downstream from nitrite reduction (Scheme 2) [42-45].”
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 [44]
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- Authors
- Fernandez, B. O., & Ford, P. C.
- Affiliations
- University of California, Santa Barbara (US)
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-08-12
- Volume
- 125
- Issue
- 35
- Pages
- 10510-10511
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2000791829
- Cited by
- 74
- References
- 18
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 2 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 4 · 2014: 6 · 2013: 4 · 2012: 4
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- 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
- reductive nitrosylation, methemoglobin, metmyoglobin, nitric oxide reduction, outer-sphere electron transfer, N2O3, nitrosating agents, protein modification
- MeSH terms
- Catalysis, Electrochemistry, Kinetics, Methemoglobin, Metmyoglobin, Nitric Oxide, Nitrites, Oxidation-Reduction
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