Title : Mutational and spectroscopic studies of the significance of the active site glutamine to metal ion specificity in superoxide dismutase.

Pub. Date : 2000 Jul 1

PMID : 11001096






8 Functional Relationships(s)
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1 We have generated a mutant of MnSOD with the active site Gln in the location characteristic of Fe-specific SODs. Glutamine superoxide dismutase 2 Homo sapiens
2 Thus, moving the active site Gln converts Mn-specific SOD into a cambialistic SOD and the Gln proves to be important but not the sole determinant of metal-ion specificity. Glutamine superoxide dismutase 2 Homo sapiens
3 Thus, moving the active site Gln converts Mn-specific SOD into a cambialistic SOD and the Gln proves to be important but not the sole determinant of metal-ion specificity. Glutamine superoxide dismutase 2 Homo sapiens
4 Thus, moving the active site Gln converts Mn-specific SOD into a cambialistic SOD and the Gln proves to be important but not the sole determinant of metal-ion specificity. Glutamine superoxide dismutase 2 Homo sapiens
5 We have directly observed the side chain of the active site Gln in Fe2+ SOD and Fe2+ (Mn)SOD by 15N NMR. Glutamine superoxide dismutase 2 Homo sapiens
6 We have directly observed the side chain of the active site Gln in Fe2+ SOD and Fe2+ (Mn)SOD by 15N NMR. Glutamine superoxide dismutase 2 Homo sapiens
7 Since a shorter distance from Gln to Fe and stronger interaction with Fe correlate with a lower Em in Fe(Mn)SOD, Gln has the effect of destabilizing additional electron density on the metal ion. Glutamine superoxide dismutase 2 Homo sapiens
8 Since a shorter distance from Gln to Fe and stronger interaction with Fe correlate with a lower Em in Fe(Mn)SOD, Gln has the effect of destabilizing additional electron density on the metal ion. Glutamine superoxide dismutase 2 Homo sapiens