Juvenile or type 2 hemochromatosis (JH) is a genetic disease caused by increased intestinal iron absorption that leads to early massive iron overload. The main form of the disease is caused by mutations in a still unknown gene on chromosome 1q. Recently, we recognized a second type of JH with clinical features identical to the 1q-linked form, caused by mutations in the gene encoding hepcidin (H...

Molecular beam studies carried out in ultrahigh vacuum show that dimethyl disulfide reacts with initially clean iron to evolve methane. The reaction is proposed to proceed via a methyl thiolate intermediate. Reaction ceases at ∼600 K, an effect that is proposed to be due to the surface being blocked by an overlayer of sulfur and carbon. Reaction recommences above ∼950 K as sulfur diffuses into ...

Protein domain movement of the Rieske iron-sulfur protein has been speculated to play an essential role in the bifurcated oxidation of ubiquinol catalyzed by the cytochrome bc1 complex. To better understand the electron transfer mechanism of the bifurcated ubiquinol oxidation at Qp site, we fixed the head domain of ISP at the cyt c1 position by creating an intersubunit disulfide bond between tw...

Hepcidin is a tightly folded 25-residue peptide hormone containing four disulfide bonds, which has been shown to act as the principal regulator of iron homeostasis in vertebrates. We used multiple techniques to demonstrate a disulfide bonding pattern for hepcidin different from that previously published. All techniques confirmed the following disulfide bond connectivity: Cys(1)-Cys(8), Cys(3)-C...

DiANNA is a recent state-of-the-art artificial neural network and web server, which determines the cysteine oxidation state and disulfide connectivity of a protein, given only its amino acid sequence. Version 1.0 of DiANNA uses a feed-forward neural network to determine which cysteines are involved in a disulfide bond, and employs a novel architecture neural network to predict which half-cystin...

Thiol/disulfide systems are involved in the maintenance of the redox status of proteins and other molecules that contain thiol/disulfide groups. Leptospirillum ferriphilum DSM14647, an acidophilic bacterium that uses Fe(2+) as electron donor, and withstands very high concentrations of iron and other redox active metals, is a good model to study how acidophiles preserve the thiol/disulfide balan...

It is essential to bear in mind that the native conformation of human proteins is stabilized by intra-molecular disulfide (S–S) bonds between a single or multiple polypeptide chains. The formation of S–S bonds is catalyzed by protein disulfide isomerase (PDI) (1), the activation of which is associated with a number of human diseases, such as myocardial infarction, stroke, and cancer. Unless pro...

use of zinc and iron oxide are common in the desulfurization process from natural gas. in thisresearch, after determinations of the size and specifications through tem and xrd for each of the metaloxides, two different size ratios were used, 0.66 for zinc oxide and 0.142 for iron oxide. further, absorption of sulfur compounds in gas (hydrogen sulfide (h2s), carbonyl sulfide (cos), methyl mercap...

Heme oxygenase (HO) catalyzes the rate-limiting step in heme catabolism to generate CO, biliverdin, and free iron. Two isoforms of HO have been identified in mammals: inducible HO-1 and constitutively expressed HO-2. HO-1 and HO-2 share similar physical and kinetic properties but have different physiological roles and tissue distributions. Unlike HO-1, which lacks cysteine residues, HO-2 contai...