Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase

Biochemistry ◽  
1979 ◽  
Vol 18 (26) ◽  
pp. 5909-5917 ◽  
Author(s):  
Douglas P. Malinowski ◽  
Irwin Fridovich
Keyword(s):  
Superoxide Dismutase ◽  
Chemical Modification ◽  
Active Site ◽  
Bovine Erythrocyte ◽  
Erythrocyte Superoxide Dismutase

scholarly journals Zinc(II) binding to apo-(bovine erythrocyte superoxide dismutase)

1979 ◽  
Vol 177 (2) ◽  
pp. 477-486 ◽  
Author(s):  
A E Cass ◽  
H A Hill ◽  
J V Bannister ◽  
W H Bannister
Keyword(s):  
Superoxide Dismutase ◽  
Binding Site ◽  
Active Site ◽  
Binding Constant ◽  
Bovine Erythrocyte ◽  
Spectral Changes ◽  
Erythrocyte Superoxide Dismutase ◽  
Order Of Magnitude ◽  
Ion Effects ◽  
Bovine Erythrocytes

The binding of zinc(II) ions to apo-(bovine erythrocytes superoxide dismutase) was studied by 1H n.m.r. spectroscopy. Two zinc(II) ions bind to each subunit of the apoenzyme, and the first has a binding constant at least an order of magnitude larger than the second. The nature of the spectral changes that occur on binding the first zinc(II) ion are interpreted in terms of a change in the structure of the protein around the active site to one very similar to that of the holoenzyme, thus pre-forming the second zinc(II) binding site. The binding of the second zinc(II) ion effects changes in the environment of only those residues involved in its co-ordination.

scholarly journals Bovine Erythrocyte Superoxide Dismutase

1974 ◽  
Vol 249 (22) ◽  
pp. 7339-7347
Author(s):  
John L. Abernethy ◽  
Howard M. Steinman ◽  
Robert L. Hill
Keyword(s):  
Superoxide Dismutase ◽  
Bovine Erythrocyte ◽  
Erythrocyte Superoxide Dismutase

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.

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