Thiocyanate and chloride as competing substrates for myeloperoxidase
Open accessAbstract
The neutrophil enzyme myeloperoxidase uses H2O2 to oxidize chloride, bromide, iodide and thiocyanate to their respective hypohalous acids. Chloride is considered to be the physiological substrate. However, a detailed kinetic study of its substrate preference has not been undertaken. Our aim was to establish whether myeloperoxidase oxidizes thiocyanate in the presence of chloride at physiological concentrations of these substrates. We determined this by measuring the rate of H2O2 loss in reactions catalysed by the enzyme at various concentrations of each substrate. The relative specificity constants for chloride, bromide and thiocyanate were 1:60:730 respectively, indicating that thiocyanate is by far the most favoured substrate for myeloperoxidase. In the presence of 100 mM chloride, myeloperoxidase catalysed the production of hypothiocyanite at concentrations of thiocyanate as low as 25 μM. With 100 μM thiocyanate, about 50% of the H2O2 present was converted into hypothiocyanite, and the rate of hypohalous acid production equalled the sum of the individual rates obtained when each of these anions was present alone. The rate of H2O2 loss catalysed by myeloperoxidase in the presence of 100 mM chloride doubled when 100 μM thiocyanate was added, and was maximal with 1 mM thiocyanate. This indicates that at plasma concentrations of thiocyanate and chloride, myeloperoxidase is far from saturated. We conclude that thiocyanate is a major physiological substrate of myeloperoxidase, regardless of where the enzyme acts. As a consequence, more consideration should be given to the oxidation products of thiocyanate and to the role they play in host defence and inflammation.
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At plasma concentrations of thiocyanate and chloride, myeloperoxidase is far from saturated.
“This indicates that at plasma concentrations of thiocyanate and chloride, myeloperoxidase is far from saturated.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [171]
The percentage of MPO-induced H2O2 loss in the presence of 100 mM Cl− doubled when 100 μM thiocyanate was added and was maximal at 1 mM thiocyanate.
“The percentage of MPO-induced H2O2 loss in the presence of 100 mM Cl− doubled when 100 µM thiocyanate was added and was maximal at 1 mM thiocyanate.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [171]
Thiocyanate is an important physiological substrate of MPO.
“Thus, thiocyanate is an important physiological substrate of MPO [170,171].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [171]
The relative specificity constants for chloride, bromide, and thiocyanate are 1:60:730, respectively, with thiocyanate being the most favoured substrate for MPO.
“The relative specificity constants for chloride, bromide, and thiocyanate are 1:60:730, respectively, with thiocyanate being the most favoured substrate for MPO.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [171]
At 100 μM thiocyanate, roughly 50% of peroxide is transformed into hypothiocyanite, and the quantity of hypohalogenic acid production was equal to the sum of the individual rates obtained when each negative ion was present alone.
“At 100 µM thiocyanate, roughly 50% of peroxide is transformed into hypothiocyanite, and the quantity of hypohalogenic acid production was equal to the sum of the individual rates obtained when each of these negative ions was present alone.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [171]
In the presence of 100 mM Cl−, MPO catalyses hypothiocyanite production at thiocyanate concentrations of 25 μM.
“In the presence of 100 mM Cl−, MPO catalyses the hypothiocyanite production at thiocyanate concentrations of 25 µM.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [171]
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- Authors
- van DALEN, J. C., WHITEHOUSE, W. M., WINTERBOURN, C. C., & KETTLE, J. A.
- Affiliations
- Free Radical Research Group, Department of Pathology, Christchurch School of Medicine, P.O. Box 4345, Christchurch, New Zealand
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1997-10-15
- Volume
- 327
- Issue
- 2
- Pages
- 487-492
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1218820
- OpenAlex
- W1768117386
- Cited by
- 406
- References
- 51
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 12 · 2023: 8 · 2022: 21 · 2021: 16 · 2020: 26 · 2019: 16 · 2018: 16 · 2017: 11 · 2016: 18 · 2015: 18 · 2014: 18 · 2013: 10 · 2012: 23
- FWCI
- 4.80
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canterbury Medical Research Foundation
- 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
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Keywords
- myeloperoxidase, thiocyanate, chloride, substrate specificity, substrate competition, hypohalous acids, hypothiocyanite, hydrogen peroxide consumption, neutrophils, hypochlorous acid, hypobromous acid, host defense, inflammation
- MeSH terms
- Binding, Competitive, Chlorides, Humans, Hydrogen Peroxide, Kinetics, Peroxidase, Neutrophils, Spectrophotometry, Substrate Specificity, Thiocyanates
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