| Abstract
| - In this paper, we investigate the effects of a point mutation on the enzymatic activity of copper−zinc superoxidedismutase, which we recently studied in detail by means of a theoretical-computational procedure (J. Phys.Chem. B2004, 108, 16255). Comparison of the reactivity of the initial catalytic steps in this mutant (G93Amutation far from the active site) with our previous data, reveals the beautiful mechanical-dynamical architectureof the enzyme, altered by such an apparently irrelevant mutation. Finally, our results suggest a possible atomic-molecular-based explanation for the mutant-pathology correlation, in line with the most recent experimentaldata.
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