Three — Dimensional Molecular Modeling, CD and Raman Studies of Plasmodium Falciparum Iron Superoxide Dismutase

1997 ◽  
pp. 53-54 ◽  
Author(s):  
Alain J. P. Alix ◽  
Manuel Dauchez ◽  
Maurice Berjot ◽  
Sylvie Grattepanche ◽  
Daniel Dive
Keyword(s):  
Superoxide Dismutase ◽  
Plasmodium Falciparum ◽  
Molecular Modeling ◽  
Three Dimensional ◽  
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.

Screening of Plasmodium falciparum iron superoxide dismutase inhibitors and accuracy of the SOD-assays

2003 ◽  
Vol 11 (23) ◽  
pp. 4941-4944 ◽  
Author(s):  
Laurent Soulère ◽  
Patrick Delplace ◽  
Elisabeth Davioud-Charvet ◽  
Sandrine Py ◽  
Christian Sergheraert ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Plasmodium Falciparum ◽  
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

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

scholarly journals Three-Dimensional Structures of Carbohydrates and Where to Find Them

2020 ◽  
Vol 21 (20) ◽  
pp. 7702 ◽  
Author(s):  
Sofya I. Scherbinina ◽  
Philip V. Toukach
Keyword(s):  
Experimental Data ◽  
Molecular Modeling ◽  
Computational Methods ◽  
Three Dimensional ◽  
Structural Diversity ◽  
Structural Data ◽  
Structural Features ◽  
Data Validation ◽  
Data Generation ◽  
Efficient Treatment

Analysis and systematization of accumulated data on carbohydrate structural diversity is a subject of great interest for structural glycobiology. Despite being a challenging task, development of computational methods for efficient treatment and management of spatial (3D) structural features of carbohydrates breaks new ground in modern glycoscience. This review is dedicated to approaches of chemo- and glyco-informatics towards 3D structural data generation, deposition and processing in regard to carbohydrates and their derivatives. Databases, molecular modeling and experimental data validation services, and structure visualization facilities developed for last five years are reviewed.

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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