in this research, a single-stage low-temperature hydrothermal synthesis route was successfully developed for preparation of iron disulfide. the prepared powder was characterized by x-ray diffraction (xrd) and scanning electron microscopy (sem). these analyses showed that nanoparticles were well crystallized, pyrite was the main product and the shape of crystals was nanorod. also, the influences...

The [2Fe-2S] cluster of the Rieske iron-sulfur protein is held between two loops of the protein that are connected by a disulfide bridge. We have replaced the two cysteines that form the disulfide bridge in the Rieske protein of Saccharomyces cerevisiae with tyrosine and leucine, and tyrosine and valine, to evaluate the effects of the disulfide bridge on assembly, stability, and thermodynamic p...

Glutaredoxins are defined as thiol disulfide oxidoreductases that reduce disulfide bonds employing reduced glutathione as electron donor. They constitute a complex family of proteins with a diversity of enzymatic and functional properties. Thus, dithiol glutaredoxins are able to reduce disulfide bonds and deglutathionylate mixed disulfides between glutathione and cysteine protein residues. They...

In this research, a single-stage low-temperature hydrothermal synthesis route was successfully developed for preparation of Iron Disulfide. The prepared powder was characterized by X-ray diffraction (XRD) and scanning electron microscopy (SEM). These analyses showed that nanoparticles were well crystallized, pyrite was the main product and the shape of crystals was nanorod. Also, the influences...

Objective: Iron is an element, which found in the structure of antioxidant enzymes and has important role inactivation reactive oxygen species. Disruption oxidant-antioxidant balance may be playing a pathogenesis iron deficiency anemia (IDA). Dynamic thiol-disulfide homeostasis (DTDH) serum ischemia-modified albumin (IMA) levels are indicators pro-oxidant/antioxidant status. In this study, we a...

Heterodisulfide reductase (Hdr) from methanogenic archea is an iron-sulfur protein that catalyzes the reversible two-electron reduction of the mixed disulfide CoM-S-S-CoB to the thiol coenzymes, coenzyme M (CoM-SH) and coenzyme B (CoB-SH). It is unusual that this enzyme uses an iron-sulfur cluster to mediate disulfide reduction in two one-electron steps via site-specific cluster chemistry. Upon...

Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a prop...

Escherichia coli thioredoxin is a small monomeric protein that reduces disulfide bonds in cytoplasmic proteins. Two cysteine residues present in a conserved CGPC motif are essential for this activity. Recently, we identified mutations of this motif that changed thioredoxin into a homodimer bridged by a [2Fe-2S] iron-sulfur cluster. When exported to the periplasm, these thioredoxin mutants could...

Synthesis and utilization of a simple copper on iron catalyst in the coupling of aryl halides with thiols through disulfide intermediate is reported. The iron support of copper catalyst ensures reductive media for the coupling, allows easy removal of the metals by outer magnetic field and enables the recycling of the catalyst.

Iron overload is the hallmark of hereditary hemochromatosis and a complication of iron-loading anemias such as β-thalassemia. Treatment can be burdensome and have significant side effects, and new therapeutic options are needed. Iron overload in hereditary hemochromatosis and β-thalassemia intermedia is caused by hepcidin deficiency. Although transgenic hepcidin replacement in mouse models of t...