Abstract
There are three types of superoxide dismutases (SOD), based on the metal involved in the catalysis {Cu(II), Fe(III) or Mn(III) in the native enzymes}. The most intensively studied protein is the copper-zinc superoxide dismutase (Cu-Zn)SOD and its metal substituted derivatives1 : an imidazolate bridging the two metal ions is the characteristic feature of the active site2. Manganese or iron SOD are a different class of proteins: X-ray crystallography data indicate that they are structural homologs characterized by a trigonal bipyramidal arrangement around the metal ion with four protein ligands and possibly a water molecule3.
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Morgenstern-Badarau, I. (1995). Magnetic and EPR Studies of Superoxide Dismutases (SOD): Electronic Structure of the Active Sites for the (Copper-Zinc)SOD, its Cobalt Substituted Derivative and the Iron(III)SOD from E. Coli . In: Kessissoglou, D.P. (eds) Bioinorganic Chemistry. NATO ASI Series, vol 459. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0255-1_10
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DOI: https://doi.org/10.1007/978-94-011-0255-1_10
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