| People | Locations | Statistics |
|---|---|---|
| Naji, M. |
| |
| Motta, Antonella |
| |
| Aletan, Dirar |
| |
| Mohamed, Tarek |
| |
| Ertürk, Emre |
| |
| Taccardi, Nicola |
| |
| Kononenko, Denys |
| |
| Petrov, R. H. | Madrid |
|
| Alshaaer, Mazen | Brussels |
|
| Bih, L. |
| |
| Casati, R. |
| |
| Muller, Hermance |
| |
| Kočí, Jan | Prague |
|
| Šuljagić, Marija |
| |
| Kalteremidou, Kalliopi-Artemi | Brussels |
|
| Azam, Siraj |
| |
| Ospanova, Alyiya |
| |
| Blanpain, Bart |
| |
| Ali, M. A. |
| |
| Popa, V. |
| |
| Rančić, M. |
| |
| Ollier, Nadège |
| |
| Azevedo, Nuno Monteiro |
| |
| Landes, Michael |
| |
| Rignanese, Gian-Marco |
|
Auchère, Françoise
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (3/3 displayed)
- 2005Superoxide reductase from the syphilis spirochete Treponema pallidum: crystallization and structure determination using soft X-rayscitations
- 2004Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the superoxide reductase neelaredoxincitations
- 2003Formation of a stable cyano-bridged dinuclear iron cluster following oxidation of the superoxide reductases from treponema pallidum and Desulfovibrio vulgaris with K3Fe(CN)6citations
Places of action
| Organizations | Location | People |
|---|
article
Formation of a stable cyano-bridged dinuclear iron cluster following oxidation of the superoxide reductases from treponema pallidum and Desulfovibrio vulgaris with K3Fe(CN)6
Abstract
<p>Superoxide reductases catalyze the monovalent reduction of superoxide anion to hydrogen peroxide. Spectroscopic evidence for the formation of a dinuclear cyano-bridged adduct after K3Fe- (CN)6 oxidation of the superoxide reductases neelaredoxin from Treponema pallidum and desulfoferrodoxin from Desulfovibrio vulgaris was reported. Oxidation with K3Fe(CN)6 reveals a band in the near-IR with, λ<sub>max</sub> at 1020 nm, coupled with an increase of the iron content by almost 2-fold. Fourier transform infrared spectroscopy provided additional evidence with CN-stretching vibrations at 2095, 2025-2030, and 2047 cm<sup>-1</sup>, assigned to a ferrocyanide adduct of the enzyme. Interestingly, the low-temperature electronic paramagnetic resonance (EPR) spectra of oxidized TpNIr reveal at least three different species indicating structural heterogeneity in the coordination environment of the active site Fe ion. Given the likely 6-coordinate geometry of the active site Fe<sup>3+</sup> ion in the ferrocyanide adduct, we propose that the rhombic EPR species can serve as a model of a hexacoordinate form of the active site.</p>