The Conserved Residue Tyrosine 34 Is Essential for Maximal Activity of Iron−Superoxide Dismutase fromEscherichia coli†

Biochemistry ◽  
1997 ◽  
Vol 36 (16) ◽  
pp. 4925-4933 ◽  
Author(s):  
Therese Hunter ◽  
Kazunori Ikebukuro ◽  
William H. Bannister ◽  
Joe V. Bannister ◽  
Gary J. Hunter
Keyword(s):  
Superoxide Dismutase ◽  
Maximal Activity ◽  
Iron Superoxide Dismutase ◽  
Fromescherichia Coli ◽  
Conserved Residue

scholarly journals The primary structure of iron superoxide dismutase fromEscherichia coli

FEBS Letters ◽  
1987 ◽  
Vol 221 (1) ◽  
pp. 87-90 ◽  
Author(s):  
M.Eugenia Schininà ◽  
Letizia Maffey ◽  
Donatella Barra ◽  
Francesco Bossa ◽  
Krystyna Puget ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Primary Structure ◽  
Iron Superoxide Dismutase ◽  
Fromescherichia Coli

Effect of Hubs in Amino Acid Network on Iron Superoxide Dismutase Stability

2015 ◽  
Vol 10 (2) ◽  
pp. 232-239
Author(s):  
Yanrui Ding ◽  
Xueqin Wang ◽  
Zhaolin Mou
Keyword(s):  
Superoxide Dismutase ◽  
Amino Acid ◽  
Iron Superoxide Dismutase

The iron content of iron superoxide dismutase: determination by anomalous scattering

1983 ◽  
Vol 218 (1210) ◽  
pp. 119-126 ◽  
Keyword(s):  
Superoxide Dismutase ◽  
Iron Content ◽  
Three Dimensional ◽  
Anomalous Scattering ◽  
Total Iron Content ◽  
Iron Site ◽  
Iron Superoxide Dismutase ◽  
Density Map ◽  
The Difference ◽  
Electron Density Map

The number of iron atoms in the dimeric iron-containing superoxide dismutase from Pseudomonas ovalis and their atomic positions have been determined directly from anomalous scattering measurements on crystals of the native enzyme. To resolve the long-standing question of the total amount of iron per molecule for this class of dismutase, the occupancy of each site was refined against the measured Bijvoet differences. The enzyme is a symmetrical dimer with one iron site in each subunit. The iron position is 9 ņ from the intersubunit interface. The total iron content of the dimer is 1.2±0.2 moles per mole of protein. This is divided between the subunits in the ratio 0.65:0.55; the difference between them is probably not significant. Since each subunit contains, on average, slightly more than half an iron atom we conclude that the normal state of this enzyme is two iron atoms per dimer but that some of the metal is lost during purification of the protein. Although the crystals are obviously a mixture of holo- and apo-enzymes, the 2.9 Å electron density map is uniformly clean, even at the iron site. We conclude that the three-dimensional structures of the iron-bound enzyme and the apoenzyme are identical.

scholarly journals A tetrameric iron superoxide dismutase from the eucaryote Tetrahymena pyriformis.

1990 ◽  
Vol 265 (29) ◽  
pp. 17680-17687
Author(s):  
D Barra ◽  
M E Schininà ◽  
F Bossa ◽  
K Puget ◽  
P Durosay ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Tetrahymena Pyriformis ◽  
Iron Superoxide Dismutase

Iron-superoxide dismutase and monodehydroascorbate reductase transcripts accumulate in response to internode rubbing in tomato

2004 ◽  
Vol 327 (7) ◽  
pp. 679-686 ◽  
Author(s):  
Ichrak Ben Rejeb ◽  
Catherine Lenne ◽  
Nathalie Leblanc ◽  
Jean-Louis Julien ◽  
Saı̈da Ammar ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Monodehydroascorbate Reductase ◽  
Iron Superoxide Dismutase
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