Superoxide dismutases: Ancient enzymes and new insights

Research output: Contribution to journalReview articlepeer-review

412 Scopus citations


Superoxide dismutases (SODs) catalyze the de toxification of superoxide. SODs therefore acquired great importance as O 2 became prevalent following the evolution of oxygenic photosynthesis. Thus the three forms of SOD provide intriguing insights into the evolution of the organisms and organelles that carry them today. Although ancient organisms employed Fe-dependent SODs, oxidation of the environment made Fe less bio-available, and more dangerous. Indeed, modern lineages make greater use of homologous Mn-dependent SODs. Our studies on the Fe-substituted MnSOD of Escherichia coli, as well as redox tuning in the FeSOD of E. coli shed light on how evolution accommodated differences between Fe and Mn that would affect SOD performance, in SOD proteins whose activity is specific to one or other metal ion.

Original languageEnglish
Pages (from-to)585-595
Number of pages11
JournalFEBS Letters
Issue number5
StatePublished - Mar 9 2012

Bibliographical note

Funding Information:
This paper is dedicated to the memory and inspiring contributions to science of Prof. A.V. Xavier. The author is grateful to the N.I.H. for funding under 1R01GM085302-01A.


  • Iron
  • Manganese
  • Proton-coupled electron transfer
  • Redox tuning
  • Superoxide dismutase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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