The peroxidase activity of mitochondrial superoxide dismutase

Kristine Ansenberger-Fricano, Douglas Ganini, Mao Mao, Saurabh Chatterjee, Shannon Dallas, Ronald P. Mason, Krisztian Stadler, Janine H. Santos, Marcelo G. Bonini*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


Manganese superoxide dismutase (MnSOD) is an integral mitochondrial protein known as a first-line antioxidant defense against superoxide radical anions produced as by-products of the electron transport chain. Recent studies have shaped the idea that by regulating the mitochondrial redox status and H 2O2 outflow, MnSOD acts as a fundamental regulator of cellular proliferation, metabolism, and apoptosis, thereby assuming roles that extend far beyond its proposed antioxidant functions. Accordingly, allelic variations of MnSOD that have been shown to augment levels of MnSOD in mitochondria result in a 10-fold increase in prostate cancer risk. In addition, epidemiologic studies indicate that reduced glutathione peroxidase activity along with increases in H2O2 further increase cancer risk in the face of MnSOD overexpression. These facts led us to hypothesize that, like its Cu,ZnSOD counterpart, MnSOD may work as a peroxidase, utilizing H 2O2 to promote mitochondrial damage, a known cancer risk factor. Here we report that MnSOD indeed possesses peroxidase activity that manifests in mitochondria when the enzyme is overexpressed.

Original languageEnglish (US)
Pages (from-to)116-124
Number of pages9
JournalFree Radical Biology and Medicine
StatePublished - Jan 2013
Externally publishedYes


  • Free radicals
  • Mitochondria
  • MnSOD
  • Overexpression
  • Peroxidase
  • SOD2

ASJC Scopus subject areas

  • Biochemistry
  • Physiology (medical)

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