Conserved enzyme-substrate electrostatic attraction in prokaryotic Cu,Zn superoxide dismutases

Biochemical and Biophysical Research Communications
S FolcarelliA Desideri

Abstract

The catalytic activity of wild type Escherichia coli Cu,Zn superoxide dismutases and of two mutants in which two lysine residues conserved in most bacterial Cu,Zn superoxide dismutases have been replaced by serine was investigated by pulse radiolysis and Brownian dynamics simulations. Experimental and computational data show that neutralization of Lys60 strongly reduces the catalytic activity of the enzyme (approximately 50%), indicating that this residue has a primary role in the electrostatic attraction of the substrate towards the catalytic copper. Neutralization of Lys63 does not significantly influence the catalytic rate constant. The results suggest that prokaryotic Cu,Zn superoxide dismutases have evolved an electrostatic mechanism to facilitate the enzyme-substrate encounter that is functionally equivalent to that already found in the eukaryotic enzymes.

Citations

Sep 29, 2004·Biological Chemistry·Roberta GabbianelliAndrea Battistoni
Jun 29, 2000·Biochemical and Biophysical Research Communications·M D'OrazioA Desideri
Jul 1, 2007·Biomolecular NMR Assignments·Beatriz JiménezMario Piccioli
Nov 25, 1998·Protein Science : a Publication of the Protein Society·F PolticelliA Desideri
Oct 11, 2005·Biochimica Et Biophysica Acta·Ivana De DomenicoAlessandro Desideri
Dec 24, 2008·Journal of Molecular Biology·Imre TöroKristina Djinović-Carugo
Jan 8, 1999·Journal of Molecular Biology·D BordoA Desideri
May 23, 2001·The Journal of Biological Chemistry·F PacelloA Battistoni
May 21, 1999·Archives of Biochemistry and Biophysics·F VeneriniA Desideri
Aug 24, 2001·International Journal of Biological Macromolecules·M BozziM Paci
Nov 1, 2005·EcoSal Plus·AndrÉs VÁzquez-Torres, Ferric C Fang

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