The DOI matches its Crossref record; 46 of the 47 references it cites were found in a registry or an index.
Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach
Abstract
Activated white cells use oxidants generated by the heme enzyme myeloperoxidase to kill invading pathogens. This enzyme utilizes H2O2 and Cl(-), Br(-), or SCN(-) to generate the oxidants HOCl, HOBr, and HOSCN, respectively. Whereas controlled production of these species is vital in maintaining good health, their uncontrolled or inappropriate formation (as occurs at sites of inflammation) can cause host tissue damage that has been associated with multiple inflammatory pathologies including cardiovascular diseases and cancer. Previous studies have reported that sulfur-containing species are major targets for HOCl but as the reactions are fast the only physiologically relevant kinetic data available have been extrapolated from data measured at high pH (>10). In this study these values have been determined at pH 7.4 using a newly developed competition kinetic approach that employs a fluorescently tagged methionine derivative as the competitive substrate (k(HOCl + Fmoc-Met), 1.5 × 10(8)M(-1)s(-1)). This assay was validated using the known k(HOCl + NADH) value and has allowed revised k values for the reactions of HOCl with Cys, N-acetylcysteine, and glutathione to be determined as 3.6 × 10(8), 2.9 × 10(7), and 1.24 × 10(8)M(-1)s(-1), respectively. Similar experiments with methionine derivatives yielded k values of 3.4 × 10(7)M(-1)s(-1) for Met and 1.7 × 10(8)M(-1)s(-1) for N-acetylmethionine. The k values determined here for the reaction of HOCl with thiols are up to 10-fold higher than those previously determined and further emphasize the critical importance of reactions of HOCl with thiol targets in biological systems.
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“HOCl reacts rapidly with several biological molecules, particularly those with thiols, thioethers, heme proteins, and amino groups, and can cause tissue injury [152].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [152]
Citations
Cites
The Acid Ionization Constant of HOCl from 5 to 35°
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Self-citationSulfur and Selenium: The Role of Oxidation State in Protein Structure and Function
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The thiol pool in human plasma: The central contribution of albumin to redox processes
Turell, L., Radí, R., & Álvarez, B. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.050 · Cited by 712
Myeloperoxidase: a front-line defender against phagocytosed microorganisms
Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0712349 · Cited by 703
Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications
Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 559
Self-citationNagy, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4973 · Cited by 503
Winterbourn, C. C. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90120-5 · Cited by 463
Quantifying the global cellular thiol–disulfide status
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Chemical kinetics and reaction mechanisms
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Cited by
Sorted by citations
Protein oxidation and peroxidation
Davies, M. J. (2016) · Biochemical Journal · doi:10.1042/bj20151227 · Cited by 952
Self-citationReactive Oxygen Species and Neutrophil Function
Winterbourn, C. C., Kettle, A. J., & Hampton, M. B. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014442 · Cited by 931
N-Acetylcysteine as an antioxidant and disulphide breaking agent: the reasons why
Aldini, G., Altomare, A., Baron, G., Vistoli, G., Carini, M., Borsani, L., & Sergio, F. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1468564 · Cited by 837
Pedre, B., Barayeu, U., Ezeriņa, D., & Dick, T. P. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107916 · Cited by 485
Redox Signaling by Reactive Electrophiles and Oxidants
Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 372
Metadata
- Authors
- Storkey, C., Davies, M. J., & Pattison, D. I.
- Affiliations
- The University of Sydney (AU)
- Corresponding author
- Pattison, David I.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 73
- Pages
- 60-66
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2000363473
- Cited by
- 165
- References
- 47
- Citations by year
- 2026: 9 · 2025: 14 · 2024: 13 · 2023: 12 · 2022: 12 · 2021: 12 · 2020: 21 · 2019: 22 · 2018: 10 · 2017: 13 · 2016: 13 · 2015: 13 · 2014: 1
- FWCI
- 6.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Australian Research Council through the Centres of Excellence (CE0561607)
- Discovery Programs (DP0988311)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- hypochlorous acid, rate constants, cysteine, methionine, thiols, glutathione, N-acetylcysteine, N-acetylmethionine, myeloperoxidase, pH 7.4, oxidative stress, inflammation, host tissue damage
- MeSH terms
- Cysteine, Hydrogen Peroxide, Hypochlorous Acid, Methionine, Peroxidase, Oxidation-Reduction, Peptides, Oxidants, Computational Biology
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