Materials Map

Discover the materials research landscape. Find experts, partners, networks.

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The Materials Map is an open tool for improving networking and interdisciplinary exchange within materials research. It enables cross-database search for cooperation and network partners and discovering of the research landscape.

The dashboard provides detailed information about the selected scientist, e.g. publications. The dashboard can be filtered and shows the relationship to co-authors in different diagrams. In addition, a link is provided to find contact information.

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Materials Map under construction

The Materials Map is still under development. In its current state, it is only based on one single data source and, thus, incomplete and contains duplicates. We are working on incorporating new open data sources like ORCID to improve the quality and the timeliness of our data. We will update Materials Map as soon as possible and kindly ask for your patience.

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in Cooperation with on an Cooperation-Score of 37%

Topics

Publications (1/1 displayed)

  • 2015Superoxide reductase from Giardia intestinalis7citations

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Chart of shared publication
Sousa, Cristiana M.
1 / 1 shared
Giuffrè, Alessandro
1 / 1 shared
Matias, Pedro M.
1 / 8 shared
Carpentier, Philippe
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Bandeiras, Tiago M.
1 / 1 shared
Pinho, Filipa
1 / 1 shared
Sarti, Paolo
1 / 1 shared
Romao, Celia
1 / 1 shared
Chart of publication period
2015

Co-Authors (by relevance)

  • Sousa, Cristiana M.
  • Giuffrè, Alessandro
  • Matias, Pedro M.
  • Carpentier, Philippe
  • Bandeiras, Tiago M.
  • Pinho, Filipa
  • Sarti, Paolo
  • Romao, Celia
OrganizationsLocationPeople

article

Superoxide reductase from Giardia intestinalis

  • Testa, Fabrizio
  • Sousa, Cristiana M.
  • Giuffrè, Alessandro
  • Matias, Pedro M.
  • Carpentier, Philippe
  • Bandeiras, Tiago M.
  • Pinho, Filipa
  • Sarti, Paolo
  • Romao, Celia
Abstract

<p>Superoxide reductase (SOR), which is commonly found in prokaryotic organisms, affords protection from oxidative stress by reducing the superoxide anion to hydrogen peroxide. The reaction is catalyzed at the iron centre, which is highly conserved among the prokaryotic SORs structurally characterized to date. Reported here is the first structure of an SOR from a eukaryotic organism, the protozoan parasite Giardia intestinalis (GiSOR), which was solved at 2.0Å resolution. By collecting several diffraction data sets at 100K from the same flash-cooled protein crystal using synchrotron X-ray radiation, photoreduction of the iron centre was observed. Reduction was monitored using an online UV-visible microspectrophotometer, following the decay of the 647nm absorption band characteristic of the iron site in the glutamate-bound, oxidized state. Similarly to other 1Fe-SORs structurally characterized to date, the enzyme displays a tetrameric quaternary-structure arrangement. As a distinctive feature, the N-terminal loop of the protein, containing the characteristic EKHxP motif, revealed an unusually high flexibility regardless of the iron redox state. At variance with previous evidence collected by X-ray crystallography and Fourier transform infrared spectroscopy of prokaryotic SORs, iron reduction did not lead to dissociation of glutamate from the catalytic metal or other structural changes; however, the glutamate ligand underwent X-ray-induced chemical changes, revealing high sensitivity of the GiSOR active site to X-ray radiation damage.</p>

Topics
  • impedance spectroscopy
  • Hydrogen
  • iron
  • Fourier transform infrared spectroscopy