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

Anne-Frances Miller

doi:10.1016/j.cbpa.2004.02.011

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

Curr Opin Chem Biol. 2004 Apr;8(2):162-8. doi: 10.1016/j.cbpa.2004.02.011.

Author

Anne-Frances Miller¹

Affiliation

¹ Department of Chemistry, University of Kentucky, Lexington KY, 40506-0055, USA. afm@uky.edu

PMID: 15062777
DOI: 10.1016/j.cbpa.2004.02.011

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 Mn3+/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 beta-sheet formation.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review

MeSH terms

Binding Sites
Oxidative Stress
Structural Homology, Protein
Superoxide Dismutase / chemistry*
Superoxide Dismutase / metabolism*

Substances

Superoxide Dismutase