Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases

Biochemistry ◽  
1979 ◽  
Vol 18 (14) ◽  
pp. 3045-3050 ◽  
Author(s):  
Glen D. Lawrence ◽  
Donald T. Sawyer
Biochemistry ◽  
1983 ◽  
Vol 22 (3) ◽  
pp. 624-627 ◽  
Author(s):  
William C. Barrette ◽  
Donald T. Sawyer ◽  
James A. Fee ◽  
Kozi Asada

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 ◽  
...  

1982 ◽  
Vol 215 (1) ◽  
pp. 116-128 ◽  
Author(s):  
Sandra L. Jewett ◽  
Gregory S. Latrenta ◽  
Carol M. Beck

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