Superoxide dismutases: Active sites that save, but a protein that kills

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296 Scopus citations

Abstract

Protection from oxidative damage is sufficiently important that biology has evolved three independent enzymes for hastening superoxide dismutation: the Cu- and Zn-containing superoxide dismutases (Cu,Zn-SODs), the SODs that are specific for Fe or Mn or function with either of the two (Fe-SODs, Mn-SODs or Fe/Mn-SODs), and the SODs that use Ni (Ni-SODs). Despite the overwhelming similarities between the active sites of Fe-SOD and Mn-SOD, the mechanisms and redox tuning of these two sites appear to incorporate crucial differences consistent with the differences between Fe3+/2+ and Mn 3+/2+. Ni-SOD is revealed by spectroscopy to employ completely different ligation to that of the other SODs while nonetheless incorporating a device also found in Cu,Zn-SOD. Finally, the protein of human Cu,Zn-SOD appears to be an important contributor to the development of amyotrophic lateral sclerosis, possibly because of its propensity for extended β-sheet formation.

Original languageEnglish
Pages (from-to)162-168
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume8
Issue number2
DOIs
StatePublished - Apr 2004

Bibliographical note

Funding Information:
I offer my belated thanks to Dr JA Fee for generosity to me at the beginning of my independent career. Work on SOD in my laboratory is currently funded by NSF MCB0129599 and the Kentucky science and engineering fund KSEF172.

Keywords

  • ALS
  • Amyotrophic lateral sclerosis
  • SOD
  • Superoxide dismutase
  • X-ray absorption spectroscopy
  • XAS

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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