Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues

Tapan Kumar Kundu, Russ Hille, Murugesan Velayutham, Jay L. Zweier

Research output: Contribution to journalArticlepeer-review

67 Scopus citations


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 ∼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.

Original languageEnglish (US)
Pages (from-to)113-121
Number of pages9
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - Apr 1 2007
Externally publishedYes


  • Aldehyde oxidase
  • Cytochrome c reduction
  • Electron paramagnetic resonance
  • Free radicals
  • Hydrogen peroxide
  • Oxygen consumption
  • Reactive oxygen species
  • Spin trapping
  • Superoxide
  • Xanthine oxidase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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