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 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 Alkylation and Identification of the Histidine Residues at the Active Site of Ribonuclease

1963 ◽  
Vol 238 (7) ◽  
pp. 2413-2420 ◽  
Author(s):  
Arthur M. Crestfield ◽  
William H. Stein ◽  
Stanford Moore
Keyword(s):  
Active Site ◽  
Histidine Residues

scholarly journals Properties and Conformation of the Histidine Residues at the Active Site of Ribonuclease

1963 ◽  
Vol 238 (7) ◽  
pp. 2421-2428 ◽  
Author(s):  
Arthur M. Crestfield ◽  
William H. Stein ◽  
Stanford Moore
Keyword(s):  
Active Site ◽  
Histidine Residues

Structure and activity of phosphoglycerate mutase

1981 ◽  
Vol 293 (1063) ◽  
pp. 121-130 ◽  
Keyword(s):  
Active Site ◽  
Transfer Reaction ◽  
Chemical Kinetic ◽  
Phosphoglycerate Mutase ◽  
Phosphoryl Transfer ◽  
X Ray ◽  
Histidine Residues ◽  
Ping Pong ◽  
Available Information ◽  
Structure And Activity

The structure of yeast phosphoglycerate mutase determined by X-ray crystallographic and amino acid sequence studies has been interpreted in terms of the chemical, kinetic and mechanistic observations made on this enzyme. There are two histidine residues at the active site, with imidazole groups almost parallel to each other and approximately 0.4 nm apart, positioned close to the 2 and 3 positions of the substrate. The simplest interpretation of the available information suggests that a ping-pong type mechanism operates in which at least one of these histidine residues participates in the phosphoryl transfer reaction. The flexible C-terminal region also plays an important role in the enzymic reaction.

A small molecular weight catalytic metalloporphyrin antioxidant with superoxide dismutase (SOD) mimetic properties protects lungs from radiation-induced injury

2002 ◽  
Vol 33 (6) ◽  
pp. 857-863 ◽  
Author(s):  
Zeljko Vujaskovic ◽  
Ines Batinic-Haberle ◽  
Zahid N Rabbani ◽  
Qin-fu Feng ◽  
Song K Kang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Superoxide Dismutase ◽  
Small Molecular Weight ◽  
Radiation Induced

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
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