scholarly journals Loss of in Vitro Metal Ion Binding Specificity in Mutant Copper-Zinc Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis

2000 ◽  
Vol 275 (2) ◽  
pp. 1007-1014 ◽  
Author(s):  
Joy J. Goto ◽  
Haining Zhu ◽  
Raylene J. Sanchez ◽  
Aram Nersissian ◽  
Edith Butler Gralla ◽  
...  
1979 ◽  
Vol 183 (1) ◽  
pp. 127-132 ◽  
Author(s):  
A E G Cass ◽  
H A O Hill ◽  
J V Bannister ◽  
W H Bannister ◽  
V Hasemann ◽  
...  

The rates of exchange of the C-2 protons of histidine residues in copper-zinc superoxide dismutase are substantially decreased by metal ion binding. This observation was used to distinguish between ligand and non ligand histidine residues in bovine and yeast copper-zinc superoxide dismutases; the effect was shown to depend only on metal ion co-ordination and not as a consequence of concomitant changes in protein structure. Selective deuteration of the zinc-only proteins at pH (uncorrected pH-meter reading) 8.2 and 50 degrees C resulted in the distinction between copper and zinc ligand resonances in the 1H n.m.r. spectrum of the enzymes. This method is proposed as a generally applicable technique for identifying histidine residues as ligands in metalloproteins.


2010 ◽  
Vol 285 (53) ◽  
pp. 41701-41711 ◽  
Author(s):  
Young-Mi Hwang ◽  
Peter B. Stathopulos ◽  
Kristin Dimmick ◽  
Hong Yang ◽  
Hamid R. Badiei ◽  
...  

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