Bacterial and eukaryotic Cu,Zn superoxide dismutases show remarkable differences in the active site region and in their quaternary structure organization. We report here a functional comparison between four Cu,Zn superoxide dismutases from Gram-negative bacteria and the eukaryotic bovine enzyme. Our data indicate that bacterial dimeric variants are characterized by catalytic rates higher than that of the bovine enzyme, probably due to the solvent accessibility of their active site. Prokaryotic Cu,Zn superoxide dismutases also show higher resistance to hydrogen peroxide inactivation and lower HCO3- -dependent peroxidative activity. Moreover, unlike the eukaryotic enzyme, all bacterial variants are susceptible to inactivation by chelating agents and show variable sensitivity to proteolytic attack, with the E. coli monomeric enzyme showing higher rates of inactivation by EDTA and proteinase K. We suggest that differences between individual bacterial variants could be due to the influence of modifications at the dimer interface on the enzyme conformational flexibility.

Gabbianelli, R., D'Orazio, M., Pacello, F., O'Neill, P., Nicolini, L., Rotilio, G., et al. (2004). Distinctive functional features in prokaryotic and eukaryotic Cu,Zn superoxide dismutases. BIOLOGICAL CHEMISTRY, 385(8), 749-754 [10.1515/BC.2004.091].

Distinctive functional features in prokaryotic and eukaryotic Cu,Zn superoxide dismutases

D'Orazio M;Pacello F;Rotilio G;Battistoni A
2004-08-01

Abstract

Bacterial and eukaryotic Cu,Zn superoxide dismutases show remarkable differences in the active site region and in their quaternary structure organization. We report here a functional comparison between four Cu,Zn superoxide dismutases from Gram-negative bacteria and the eukaryotic bovine enzyme. Our data indicate that bacterial dimeric variants are characterized by catalytic rates higher than that of the bovine enzyme, probably due to the solvent accessibility of their active site. Prokaryotic Cu,Zn superoxide dismutases also show higher resistance to hydrogen peroxide inactivation and lower HCO3- -dependent peroxidative activity. Moreover, unlike the eukaryotic enzyme, all bacterial variants are susceptible to inactivation by chelating agents and show variable sensitivity to proteolytic attack, with the E. coli monomeric enzyme showing higher rates of inactivation by EDTA and proteinase K. We suggest that differences between individual bacterial variants could be due to the influence of modifications at the dimer interface on the enzyme conformational flexibility.
ago-2004
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Superoxide Dismutase; Animals; Hydrogen Peroxide; Photobacterium; Salmonella typhimurium; Binding Sites; Cattle; Kinetics; Eukaryotic Cells; Edetic Acid; Oxidants; Prokaryotic Cells; Catalysis; Protein Conformation
Gabbianelli, R., D'Orazio, M., Pacello, F., O'Neill, P., Nicolini, L., Rotilio, G., et al. (2004). Distinctive functional features in prokaryotic and eukaryotic Cu,Zn superoxide dismutases. BIOLOGICAL CHEMISTRY, 385(8), 749-754 [10.1515/BC.2004.091].
Gabbianelli, R; D'Orazio, M; Pacello, F; O'Neill, P; Nicolini, L; Rotilio, G; Battistoni, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/31439
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