TY - JOUR
T1 - Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of trypanosoma cruzi iron-superoxide dismutases (fe-sods) a and b
T2 - Disparate susceptibilities due to the repair of tyr35 radical by cys83 in fe-sodb through intramolecular electron transfer
AU - Martinez, Alejandra
AU - Peluffo, Gonzalo
AU - Petruk, Ariel A.
AU - Hugo, Martín
AU - Piñeyro, Dolores
AU - Demicheli, Verónica
AU - Moreno, Diego M.
AU - Lima, Analía
AU - Batthyány, Carlos
AU - Durán, Rosario
AU - Robello, Carlos
AU - Martí, Marcelo A.
AU - Larrieux, Nicole
AU - Buschiazzo, Alejandro
AU - Trujillo, Madia
AU - Radi, Rafael
AU - Piacenza, Lucía
PY - 2014
Y1 - 2014
N2 - Background: Superoxide dismutases are inactivated by peroxynitrite. Results: T. cruzi cytosolic Fe-SODB is highly resistant toward peroxynitrite-mediated tyrosine nitration and inactivation as compared with mitochondrial Fe-SODA. Conclusion: Intramolecular electron transfer in Fe-SODB from Cys83 to critical Tyr35 prevents enzyme nitration and inactivation. Significance: Disparate susceptibilities of Fe-SODs to peroxynitrite can influence parasite virulence during T. cruzi infection of mammalian cells.
AB - Background: Superoxide dismutases are inactivated by peroxynitrite. Results: T. cruzi cytosolic Fe-SODB is highly resistant toward peroxynitrite-mediated tyrosine nitration and inactivation as compared with mitochondrial Fe-SODA. Conclusion: Intramolecular electron transfer in Fe-SODB from Cys83 to critical Tyr35 prevents enzyme nitration and inactivation. Significance: Disparate susceptibilities of Fe-SODs to peroxynitrite can influence parasite virulence during T. cruzi infection of mammalian cells.
UR - https://www.scopus.com/pages/publications/84899752756
U2 - 10.1074/jbc.M113.545590
DO - 10.1074/jbc.M113.545590
M3 - Article
C2 - 24616096
AN - SCOPUS:84899752756
SN - 0021-9258
VL - 289
SP - 12760
EP - 12778
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 18
ER -