The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites.
Open accessAbstract
The reactions of human hemoglobin with sodium nitrite and ethyl nitrite in deoxygenated media have been examined in kinetic detail. Nitrous acid has been identified from kinetic pH dependence studies as the principal oxidant of hemoglobin in reactions with sodium nitrite. Nitrosylhemoglobin is produced concurrently with methemoglobin as a result of reductive release of nitric oxide from nitrous acid. However, oxidation of hemoglobin by nitric oxide competes with association, and this process is proposed to arise from the action of the nitric oxide dimer on hemoglobin. Ethyl nitrite, which serves as a model for nitrous acid, reacts with hemoglobin at rates that are at least 10 times slower than those extrapolated for nitrous acid, and hydrolysis of the alkyl nitrite is not competitive with oxidation of hemoglobin. The composite experimental results are interpreted to describe alkyl nitrite, and, presumably, nitrous acid association with hemoglobin followed by rate-limiting electron transfer resulting in nitric oxide and alkoxide (or hydroxide) production. Proton transfer resulting in alcohol (or water) formation occurs subsequent to the rate-limiting step as do reactions of hemoglobin with nitric oxide.
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In the citing paper
“By studying the same reaction using alkyl nitrites, which do not show a pH dependence in their reaction rates with deoxyHb, it was established that the reaction of nitrite requires a proton and thus formally requires nitrous acid (247, 248). This property also makes the reaction faster in low pH conditions.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [248]
In the citing paper
“This scheme has been found to apply to virtually all the heme protein–mediated nitrite reduction reactions studied to date, including Hb (248, 447), Mb (247, 862), neuroglobin (Ngb) (932, 945), Cygb (182, 571, 780), cystathionine β-synthase (CBS) (149, 350), globin X (184), plant and cyanobacterial Hb (phytohemoglobins) (905, 946), flavohemoglobin (340), heme-albumin (43), cytochrome c (41), prot”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [248]
In the citing paper
“In the acute setting, nitrite can bind to hemoglobin and oxidize the ferrous iron in heme to the ferric state, thereby forming methemoglobin (metHgb) and preventing the binding of oxygen[152].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [152]
In the citing paper
“(1)NO2−+HbFe2++H+→NO+HbFe3++OH−”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [35]
In the citing paper
“Doyle and colleagues found k0 to be 12.3 × 103 M−1s−1 [35].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [35]
In the citing paper
“The dependence on pH is likely due to the heme actually predominately reacting with nitrous acid, HONO, rather than the nitrite anion.”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [35]
Citations
Cites
Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins
Doyle, M. P., & Hoekstra, J. W. (1981) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80291-3 · Cited by 643
Self-citationReactions of nitric oxide coordinated to transition metals
McCleverty, J. A. (1979) · Chemical Reviews · doi:10.1021/cr60317a005 · Cited by 305
METHEMOGLOBINEMIA AND METHEMOGLOBIN-PRODUCING COMPOUNDS
Bodansky, O. (1951) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)07311-9 · Cited by 299
Cooperativity in the dissociation of nitric oxide from hemoglobin.
Moore, E. G., & Gibson, Q. H. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33557-3 · Cited by 292
Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
Perutz, M. F., Ladner, J. E., Simon, S. R., & Ho, C. (1974) · Biochemistry · doi:10.1021/bi00707a026 · Cited by 292
Conformation, co-operativity and ligand binding in human hemoglobin
Cassoly, R., & Gibson, Q. H. (1975) · Journal of Molecular Biology · doi:10.1016/0022-2836(75)90382-4 · Cited by 259
Kiese, M. (1966) · PubMed · Cited by 200
The toxicology of nitrate, nitrite and n‐nitroso compounds
SWANN, P. F. (1975) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.2740261119 · Cited by 168
Austin, J. H., & Drabkin, D. L. (1935) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)74966-1 · Cited by 156
Banerjee, R., Alpert, Y., Leterrier, F., & Williams, R. J. P. (1969) · Biochemistry · doi:10.1021/bi00835a025 · Cited by 111
Research works printed but not linked: 4
- Kiese, 1966, Pharmacol. Rev., 18, 1091, 10.1016/S0031-6997(25)07167-4 · DOI
- Sherman, 1979, Am. J. Dis. Child, 133, 439
- Chalamet, 1973, Ann. Chim., 8, 353
- LeMaistre, J. W. (1972) in Study Syst., Coronary Myocardial Effects of Nitrates, Proceedings Symposium, 1970, pp. 251–257
Cited by
Sorted by citations
The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics
Lundberg, J. O., Weitzberg, E., & Gladwin, M. T. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2466 · Cited by 2,739
Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation
Cosby, K., Partovi, K. S., Crawford, J. H., Patel, R. P., Reiter, C. D., Martyr, S., Yang, B. K., Waclawiw, M. A., Zalos, G., Xu, X., et al. (2003) · Nature Medicine · doi:10.1038/nm954 · Cited by 1,807
Nitric oxide synthase in innate and adaptive immunity: an update
Bogdan, C. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.01.003 · Cited by 862
Riess, J. G. (2001) · Chemical Reviews · doi:10.1021/cr970143c · Cited by 787
Nitrate, bacteria and human health
Lundberg, J. O., Weitzberg, E., Cole, J. A., & Benjamin, N. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro929 · Cited by 739
Metadata
- Authors
- Doyle, M. P., Pickering, R. A., DeWeert, T. M., Hoekstra, J. W., & Pater, D.
- Affiliations
- Hope College (US)
- ORCID
- Doyle, M.P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1981-12
- Volume
- 256
- Issue
- 23
- Pages
- 12393-12398
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1589586351
- Cited by
- 334
- References
- 37
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 5 · 2023: 4 · 2022: 2 · 2021: 10 · 2020: 4 · 2019: 8 · 2018: 12 · 2017: 7 · 2016: 12 · 2015: 18 · 2014: 16 · 2013: 11 · 2012: 12
- FWCI
- 0.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- nitrous acid, sodium nitrite, ethyl nitrite, nitric oxide, nitrosylhemoglobin, methemoglobin, nitric oxide dimer, electron transfer, reaction mechanism, reaction kinetics, proton transfer
- MeSH terms
- Hemoglobin A, Humans, Hydrogen-Ion Concentration, Kinetics, Nitrites, Oxidation-Reduction, Oxyhemoglobins, Sodium Nitrite, Spectrophotometry
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