Selective Deuteration of Histidine Residues in Bovine Superoxide Dismutase

1979 ◽  
Vol 7 (4) ◽  
pp. 716-717 ◽  
Author(s):  
ANTHONY E. G. CASS ◽  
H. ALLEN O. HILL ◽  
WILLIAM H. BANNISTER ◽  
JOSEPH V. BANNISTER
Keyword(s):  
Superoxide Dismutase ◽  
Histidine Residues ◽  
Selective Deuteration

scholarly journals Disease-associated Mutations at Copper Ligand Histidine Residues of Superoxide Dismutase 1 Diminish the Binding of Copper and Compromise Dimer Stability

2006 ◽  
Vol 282 (1) ◽  
pp. 345-352 ◽  
Author(s):  
Jiou Wang ◽  
Amy Caruano-Yzermans ◽  
Angela Rodriguez ◽  
Jonathan P. Scheurmann ◽  
Hilda H. Slunt ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Dismutase 1 ◽  
Histidine Residues

scholarly journals Investigation of human erythrocyte superoxide dismutase by 1H nuclear-magnetic-resonance spectroscopy

1980 ◽  
Vol 185 (1) ◽  
pp. 245-252 ◽  
Author(s):  
H A O Hill ◽  
W K Lee ◽  
J V Bannister ◽  
W H Bannister
Keyword(s):  
Superoxide Dismutase ◽  
Active Site ◽  
Human Erythrocyte ◽  
Superoxide Dismutases ◽  
Resonance Spectroscopy ◽  
Structural Homology ◽  
Histidine Residues ◽  
Erythrocyte Superoxide Dismutase ◽  
1H Nuclear Magnetic Resonance ◽  
Acetyl Group

The 170MHZ 1 H n.m.r. spectra of the Cu(II)/Zn(II), Cu(I)/Zn(II) and apo- forms of human erythrocyte superoxide dismutase (EC 1.15.1.1) are reported. Resonances are assigned to the C-2 and C-4 protons of histidine residues in the active site, and it is suggested that five or six histidine residues serve as ligands to the metal ions in each subunit of the enzyme. The remaining assigned resonances are associated with histidine-41, N-terminal N-acetyl group, histidine- 108 and cysteine- 109. A comparison of the n.m.r. spectra of human and bovine superoxide dismutases suggests significant structural homology.

scholarly journals The exchange of histidine C-2 protons in superoxide dismutases. A novel method for assigning histidine-metal ligands in proteins

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 ◽  
...  
Keyword(s):  
Metal Ion ◽  
Superoxide Dismutases ◽  
Metal Ion Binding ◽  
Histidine Residues ◽  
Copper Zinc Superoxide Dismutase ◽  
Metal Ligands ◽  
Zinc Superoxide Dismutase ◽  
Selective Deuteration ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases

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.

Superoxide Dismutase Inactivation by Radiation-Induced Radicals: Evidence for Histidine Residues in the Active Site

1974 ◽  
Vol 60 (3) ◽  
pp. 441 ◽  
Author(s):  
P. B. Roberts ◽  
E. M. Fielden ◽  
G. Rotilio ◽  
L. Calabrese ◽  
J. V. Bannister ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Active Site ◽  
Histidine Residues ◽  
Radiation Induced

scholarly journals Studies of the limited degradation of mucus glycoproteins. The mechanism of the peroxide reaction

1985 ◽  
Vol 228 (3) ◽  
pp. 615-626 ◽  
Author(s):  
B Cooper ◽  
J M Creeth ◽  
A S Donald
Keyword(s):  
Superoxide Dismutase ◽  
Acetic Acid ◽  
Metal Ion ◽  
Histidine Residues ◽  
Essential Step ◽  
Oxidation Reduction ◽  
Reduction Cycle ◽  
Metal Ion Catalysis ◽  
Chelex Resin ◽  
Mucus Glycoproteins

The reaction between ovarian-cyst glycoproteins and H2O2 was investigated in the presence of a number of inhibitors and catalysts. Azide and 2H2O were separately found to have little effect, implying that singlet oxygen was not involved. Superoxide dismutase was destroyed by H2O2, but mannitol had no effect: thus generalized attack by OH., whether originating from HO2.- or more directly, is not indicated. The glycoproteins contained trace quantities of Cu and Fe, amounting to about 2 atoms of metal per glycoprotein molecule. Treatment of the glycoproteins with the strong chelator DETAPAC (diethylenetriaminepenta-acetic acid) or Chelex resin eliminated the reaction with H2O2; activity could be restored by addition of Cu2+ or Fe2+ in millimolar quantities. It was concluded that metal-ion catalysis is an essential step in the attack of H2O2 on glycoproteins. Spectroscopic and other evidence showed that Cu2+ (and probably Fe2+) complexes strongly with poly-L-histidine, and implies that the Cu2+ or Fe2+ in the glycoproteins is complexed with some of the histidine residues in the glycosylated backbone. Neither polyhistidine nor polyproline reacted with H2O2 in the absence of metal ions, but small quantities of Cu2+ or Fe3+ caused degradation. This was rapid with polyhistidine, which was converted largely into aspartic acid, but slower with polyproline, where limited conversion into glutamic acid occurs. These findings confirm the original hypothesis that peroxide attack on glycoproteins occurs largely at the histidine residues, with simultaneous peptidolysis. The mechanism most probably involves the liberation of OH. by an oxidation-reduction cycle involving, e.g. Cu+/Cu2+: specificity of attack at histidine is due to the location of the metal at these residues only.

scholarly journals Oxidation of Histidine Residues in Copper−Zinc Superoxide Dismutase by Bicarbonate-Stimulated Peroxidase and Thiol Oxidase Activities: Pulse EPR and NMR Studies

Biochemistry ◽  
2010 ◽  
Vol 49 (50) ◽  
pp. 10616-10622 ◽  
Author(s):  
Karunakaran Chandran ◽  
John McCracken ◽  
Francis C. Peterson ◽  
William E. Antholine ◽  
Brian F. Volkman ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Nmr Studies ◽  
Histidine Residues ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Pulse Epr ◽  
Copper Zinc ◽  
Thiol Oxidase

scholarly journals Changes in the histidine residues of Cu/Zn superoxide dismutase during aging

FEBS Letters ◽  
1995 ◽  
Vol 374 (1) ◽  
pp. 85-88 ◽  
Author(s):  
Consuelo Santa Maria ◽  
Elisa Revilla ◽  
Antonio Ayala ◽  
Cristina P. de la Cruz ◽  
Alberto Machado
Keyword(s):  
Superoxide Dismutase ◽  
Histidine Residues
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