scholarly journals Geometric and Electronic Structures of Manganese-Substituted Iron Superoxide Dismutase

2013 ◽  
Vol 52 (6) ◽  
pp. 3356-3367 ◽  
Author(s):  
Timothy A. Jackson ◽  
Craig T. Gutman ◽  
James Maliekal ◽  
Anne-Frances Miller ◽  
Thomas C. Brunold
Keyword(s):  
Superoxide Dismutase ◽  
Electronic Structures ◽  
Iron Superoxide Dismutase

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

Cloning, Expression, and Characterization of Iron Superoxide Dismutase in Sonneratia alba, a Highly Salt Tolerant Mangrove Tree

2013 ◽  
Vol 32 (4) ◽  
pp. 259-265 ◽  
Author(s):  
Feng Wang ◽  
Qiuhong Wu ◽  
Zide Zhang ◽  
Shufang Chen ◽  
Renchao Zhou
Keyword(s):  
Superoxide Dismutase ◽  
Salt Tolerant ◽  
Iron Superoxide Dismutase ◽  
Mangrove Tree ◽  
Sonneratia Alba

Protection of Methanosarcina barkeri against oxidative stress: identification and characterization of an iron superoxide dismutase

2000 ◽  
Vol 174 (3) ◽  
pp. 213-216 ◽  
Author(s):  
Andrei Brioukhanov ◽  
Alexander Netrusov ◽  
Melanie Sordel ◽  
Rudolf K. Thauer ◽  
Seigo Shima
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Methanosarcina Barkeri ◽  
Iron Superoxide Dismutase ◽  
Identification And Characterization

scholarly journals Cloned Prokaryotic Iron Superoxide Dismutase Protects Yeast Cells against Oxidative Stress Depending on Mitochondrial Location

1999 ◽  
Vol 256 (1) ◽  
pp. 63-67 ◽  
Author(s):  
Rena Balzan ◽  
Dolores R Agius ◽  
William H Bannister
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Yeast Cells ◽  
Iron Superoxide Dismutase
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