Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues
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Aldehyde oxidase, a molybdoflavoenzyme that plays an important role in aldehyde biotransformation, requires oxygen as substrate and produces reduced oxygen species. However, little information is available regarding its importance in cellular redox stress. Therefore, studies were undertaken to characterize its superoxide and hydrogen peroxide production. Aldehyde oxidase was purified to >98% purity and exhibited a single band at approximately 290 kDa on native polyacrylamide gradient gel electrophoresis. Superoxide generation was measured and quantitated by cytochrome c reduction and EPR spin trapping with p-dimethyl aminocinnamaldehyde as reducing substrate. Prominent superoxide generation was observed with an initial rate of 295 nmol min(-1) mg(-1). Electrochemical measurements of oxygen consumption and hydrogen peroxide formation yielded values of 650 and 355 nmol min(-1) mg(-1). In view of the ubiquitous distribution of aldehydes in tissues, aldehyde oxidase can be an important basal source of superoxide that would be enhanced in disease settings where cellular aldehyde levels are increased.
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Lipoxygenases are biological sources of superoxide.
“Lipoxygenases catalyze the insertion of oxygen in polyunsaturated fatty acids (119, 535, 1040) and are also biological sources of superoxide (537).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [537]
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- Authors
- Kundu, T. K., Hille, R., Velayutham, M., & Zweier, J. L.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Zweier, Jay L.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2007-04
- Volume
- 460
- Issue
- 1
- Pages
- 113-121
- ISSN
- 0003-9861 (ISSN-L)
- PMC
- PMC4073616
- OpenAlex
- W2091194381
- Cited by
- 83
- References
- 61
- Citations by year
- 2026: 1 · 2024: 3 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 7 · 2018: 5 · 2017: 8 · 2016: 6 · 2015: 2 · 2014: 12 · 2013: 5 · 2012: 9
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL-38324, R01HL063744, HL 65608, P01HL065608, HL 63744, R01HL038324)
- National Institute of General Medical Sciences (GM 075036, R01GM075036)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
- Keywords
- aldehyde oxidase, superoxide production, hydrogen peroxide, oxygen consumption, cytochrome c reduction, EPR spin trapping, p-dimethylaminocinnamaldehyde, enzyme purification
- MeSH terms
- Animals, Hydrogen Peroxide, Liver, Male, Oxidation-Reduction, Oxygen Consumption, Superoxides, Time Factors, Oxidants, Rats, Sprague-Dawley, Spin Trapping, Aldehyde Oxidase, Cytochromes c, Rats
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