scholarly journals Carbon-2 proton exchange at histidine-41 in bovine erythrocyte superoxide dismutase

1977 ◽  
Vol 165 (3) ◽  
pp. 587-589 ◽  
Author(s):  
A E G Cass ◽  
H A O Hill ◽  
B E Smith ◽  
J V Bannister ◽  
W H Bannister

The C-2 proton of one histidine residue in bovine erythrocyte superoxide dismutase is shown to be particularly labile. This residue is identified by tritiation, protein digestion and subsequent peptide ‘mapping’ as histidine-41. A half-life for the exchange of histidine C-2 1H for 2H in 2H2O as solvent, at pD 8.1 and 40 degrees C, is estimated as approx. 9.2h, 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

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.


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

Sign in / Sign up

Export Citation Format

Share Document