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Biophys J, June 2001, p. 2556-2567, Vol. 80, No. 6

Dynamics-Function Correlation in Cu, Zn Superoxide Dismutase: A Spectroscopic and Molecular Dynamics Simulation Study

M. Falconi,* M. E. Stroppolo,* P. Cioni,dagger G. Strambini,dagger A. Sergi,Dagger M. Ferrario,§ and A. Desideri*

 *INFM and Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica, 00133, Rome, Italy.  dagger Istituto di Biofisica CNR, Pisa;  Dagger INFM and Department of Physics, University of Rome "La Sapienza", 00185 Rome; and  §INFM Department of Physics, University of Modena, 41100 Modena, Italy.

A single mutation (Val29right-arrowGly) at the subunit interface of a Cu, Zn superoxide dismutase dimer leads to a twofold increase in the second order catalytic rate, when compared to the native enzyme, without causing any modification of the structure or the electric field distribution (Stroppolo et al., 2000). To check the role of dynamic processes in this catalytic enhancement, the flexibility of the dimeric protein at the subunit interface region has been probed by the phosphorescence and fluorescence properties of the unique tryptophan residue. Multiple spectroscopic data indicate that Trp83 experiences a very similar, and relatively hydrophobic, environment in both wild-type and mutant protein, whereas its mobility is distinctly more restrained in the latter. Molecular dynamics simulation confirms this result, and provides, at the molecular level, details of the dynamic change felt by tryptophan. Moreover, the simulation shows that the loops surrounding the active site are more flexible in the mutant than in the native enzyme, making the copper more accessible to the incoming substrate, and being thus responsible for the catalytic rate enhancement. Evidence for increased, dynamic copper accessibility also comes from faster copper removal in the mutant by a metal chelator. These results indicate that differences in dynamic, rather than structural, features of the two enzymes are responsible for the observed functional change.

Biophys J, June 2001, p. 2556-2567, Vol. 80, No. 6
© 2001 by the Biophysical Society   0006-3495/01/06/2556/12  $2.00


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