The Role of Superoxide Anion in the Autoxidation of Epinephrine and a Simple Assay for Superoxide Dismutase
Open accessAbstract
The rate of autoxidation of epinephrine and the sensitivity of this autoxidation to inhibition by superoxide dismutase were both augmented, as the pH was raised from 7.8 → 10.2. O2-, generated by the xanthine oxidase reaction, caused the oxidation of epinephrine to adrenochrome and the yield of adrenochrome produced per O2- introduced, increased with increasing pH in the range 7.8 → 10.2 and also increased with increasing concentration of epinephrine. These results, in conjunction with complexities in the kinetics of adrenochrome accumulation, lead to the proposal that the autoxidation of epinephrine proceeds by at least two distinct pathways, only one of which is a free radical chain reaction involving O2- and hence inhibitable by superoxide dismutase. This chain reaction accounted for a progressively greater fraction of the total oxidation as the pH was raised. The ability of superoxide dismutase to inhibit the autoxidation of epinephrine at pH 10.2 has been used as the basis of a convenient and sensitive assay for this enzyme.
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In some assays, O2 reduces tetranitro methane, cytochrome c or nitro tetrazolium blue, and in others it oxidises epinephrine, tiron pyrogallol or 6-hydroxydopamine.
“Thus, in some assays, Oz reduces tetranitro methane [11], cytochrome c or nitro tetrazolium blue [100], and in others it oxidises epinephrine, tiron pyrogallol or 6-hydroxydopamine [101,102], Figure 38.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [101]
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- Authors
- Misra, H. P., & Fridovich, I.
- Affiliations
- Duke Medical Center (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1972-05
- Volume
- 247
- Issue
- 10
- Pages
- 3170-3175
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1750690213
- Cited by
- 9,097
- References
- 1
- Citations by year
- 2026: 329 · 2025: 438 · 2024: 471 · 2023: 495 · 2022: 524 · 2021: 541 · 2020: 525 · 2019: 422 · 2018: 411 · 2017: 405 · 2016: 371 · 2015: 358 · 2014: 380 · 2013: 358 · 2012: 314
- FWCI
- 13.11
- 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 › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- superoxide, superoxide dismutase, adrenochrome, xanthine oxidase, free radical chain reaction, pH dependence, enzyme activity assay
- MeSH terms
- Adrenochrome, Animals, Catalase, Cattle, Edetic Acid, Epinephrine, Erythrocytes, Escherichia coli, Free Radicals, Hydrogen-Ion Concentration, Kinetics, Oxidation-Reduction, Oxidoreductases, Oxygen, Polarography, Spectrophotometry, Xanthine Oxidase, Yeasts
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