PMID:15260508

Citation	Jackson, TA and Brunold, TC (2004) Combined spectroscopic/computational studies on Fe- and Mn-dependent superoxide dismutases: insights into second-sphere tuning of active site properties. Acc. Chem. Res. 37:461-70
Abstract	Superoxide dismutases (SODs) are metalloenzymes that protect aerobic organisms from oxidative damage mediated by the superoxide radical. While the Fe- and Mn-dependent SODs from E. coli possess virtually identical protein folds and active-site geometries, they are strictly metal specific. To explore the origin of this extraordinary metal-ion specificity and to elucidate the mechanisms by which these enzymes tune the geometric and electronic properties, and thus the reactivity, of their active-site metal ions, we utilized a combination of spectroscopic and computational methods to study the native enzymes, their metal-substituted derivatives, and several mutant proteins. Results from our research described in this Account reveal that second-sphere residues are critically involved in controlling both thermodynamic and kinetic properties of the Fe- and MnSOD active sites.
Links	PubMed Online version:10.1021/ar030272h
Keywords	Binding Sites; Circular Dichroism; Computational Biology; Iron/chemistry; Kinetics; Manganese/chemistry; Models, Molecular; Oxidation-Reduction; Oxygen/metabolism; Superoxide Dismutase/chemistry; Superoxide Dismutase/metabolism
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