The three-dimensional structure of Cu,Zn superoxide dismutase (SOD) from the shark Prionace glauca was homology modeled on the structure of the bovine enzyme used as a template. Shark SOD displays the conservative substitution of one of the residues involved in the electrostatic guidance of superoxide toward the active site of the enzyme, i.e., Lys134, which is replaced by arginine. The association rate, calculated by brownian dynamics simulations incorporating electrostatic terms, and the enzyme reaction rate, measured by the pulse radiolysis method, were found to be identical for both bovine and shark SODs. In order to quantify the role of Lys134 in electrostatically steering the superoxide to the active site, chemical modification of the lysine residues by carbamoylation was carried out on both bovine and shark. SODs. Experimental determination of the enzymatic reaction rate indicated that the charge located on the residue 134 gives 19% contribution to the guidance of superoxide anion at low ionic strength. This value matches the association rates predicted by brownian dynamics. (C) 1994 Academic Press, Inc.

Polticelli, F., Falconi, M., Oneill, P., Petruzelli, R., Galtieri, A., Lania, A., et al. (1994). MOLECULAR MODELING AND ELECTROSTATIC POTENTIAL CALCULATIONS ON CHEMICALLY-MODIFIED CU,ZN SUPEROXIDE DISMUTASES FROM BOS-TAURUS AND SHARK PRIONACE GLAUCA - ROLE OF LYS134 IN ELECTROSTATICALLY STEERING THE SUBSTRATE TO THE ACTIVE-SITE RID A-4573-2009. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 312(1), 22-30 [10.1006/abbi.1994.1275 WC Biochemistry & Molecular Biology; Biophysics].

MOLECULAR MODELING AND ELECTROSTATIC POTENTIAL CALCULATIONS ON CHEMICALLY-MODIFIED CU,ZN SUPEROXIDE DISMUTASES FROM BOS-TAURUS AND SHARK PRIONACE GLAUCA - ROLE OF LYS134 IN ELECTROSTATICALLY STEERING THE SUBSTRATE TO THE ACTIVE-SITE RID A-4573-2009

POLTICELLI, Fabio;
1994-01-01

Abstract

The three-dimensional structure of Cu,Zn superoxide dismutase (SOD) from the shark Prionace glauca was homology modeled on the structure of the bovine enzyme used as a template. Shark SOD displays the conservative substitution of one of the residues involved in the electrostatic guidance of superoxide toward the active site of the enzyme, i.e., Lys134, which is replaced by arginine. The association rate, calculated by brownian dynamics simulations incorporating electrostatic terms, and the enzyme reaction rate, measured by the pulse radiolysis method, were found to be identical for both bovine and shark SODs. In order to quantify the role of Lys134 in electrostatically steering the superoxide to the active site, chemical modification of the lysine residues by carbamoylation was carried out on both bovine and shark. SODs. Experimental determination of the enzymatic reaction rate indicated that the charge located on the residue 134 gives 19% contribution to the guidance of superoxide anion at low ionic strength. This value matches the association rates predicted by brownian dynamics. (C) 1994 Academic Press, Inc.
Polticelli, F., Falconi, M., Oneill, P., Petruzelli, R., Galtieri, A., Lania, A., et al. (1994). MOLECULAR MODELING AND ELECTROSTATIC POTENTIAL CALCULATIONS ON CHEMICALLY-MODIFIED CU,ZN SUPEROXIDE DISMUTASES FROM BOS-TAURUS AND SHARK PRIONACE GLAUCA - ROLE OF LYS134 IN ELECTROSTATICALLY STEERING THE SUBSTRATE TO THE ACTIVE-SITE RID A-4573-2009. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 312(1), 22-30 [10.1006/abbi.1994.1275 WC Biochemistry & Molecular Biology; Biophysics].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11590/137968
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