3 documents found, page 1 of 1

Sort by Issue Date

Interaction of [(VO)-O-IV(acac)(2)] with Human Serum Transferrin and Albumin

Correia, Isabel; Chorna, Ielyzaveta; Cavaco, Isabel; Roy, Somnath; Kuznetsov, Maxim L.; Ribeiro, Nadia; Justino, Goncalo; Marques, Fernanda

VO(acac)(2)] is a remarkable vanadium compound and has potential as a therapeutic drug. It is important to clarify how it is transported in blood, but the reports addressing its binding to serum proteins have been contradictory. We use several spectroscopic and mass spectrometric techniques (ESI and MALDI-TOF), small-angle X-ray scattering and size exclusion chromatography (SEC) to characterize solutions contai...


The first crystal structure of class III superoxide reductase from Treponema pa...

Santos-Silva, Teresa; Trincão, José; Carvalho, Ana Luísa; Bonifácio, Cecília; Auchère, Françoise; Raleiras, Patrícia; Moura, Isabel; Moura, José J. G.

J Biol Inorg Chem (2006) 11: 548–558 DOI 10.1007/s00775-006-0104-y; Superoxide reductase (SOR) is a metalloprotein containing a non-heme iron centre, responsible for the scavenging of superoxide radicals in the cell. The crystal structure of Treponema pallidum (Tp) SOR was determined using soft X-rays and synchrotron radiation. Crystals of the oxidized form were obtained using poly(ethylene glycol) and MgCl2 an...


Superoxide reductase from the syphilis spirochete Treponema pallidum

Moura, Isabel; Santos-Silva, Teresa; Trincão, José; Carvalho, Ana L.; Auchère, Françoise; Moura, José J. G.; Romão, Maria J.

Superoxide reductase is a 14 kDa metalloprotein containing a catalytic nonhaem iron centre [Fe(His)4Cys]. It is involved in defence mechanisms against oxygen toxicity, scavenging superoxide radicals from the cell. The oxidized form of Treponema pallidum superoxide reductase was crystallized in the presence of polyethylene glycol and magnesium chloride. Two crystal forms were obtained depending on the oxidizing ...


3 Results

Queried text

Refine Results

Author





















Date




Document Type


Access rights


Resource



Subject