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Sulphur pathway

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Benzyl isothiocyanate disturbs lipid metab... [J Physiol Biochem. 2012. Thiocyanate. Thiocyanate is analogous to the cyanate ion, [OCN]−, wherein oxygen is replaced by sulfur. [SCN]− is one of the pseudohalides, due to the similarity of its reactions to that of halide ions. Thiocyanate used to be known as rhodanide (from a Greek word for rose) because of the red colour of its complexes with iron. Thiocyanate is produced by the reaction of elemental sulfur or thiosulfate with cyanide: The second reaction is catalyzed by the enzyme sulfotransferase known as rhodanase and may be relevant to detoxification of cyanide in the body.

Structure, bonding and coordination chemistry[edit] Thiocyanate shares its negative charge approximately equally between sulfur and nitrogen. As a consequence, thiocyanate can act as a nucleophile at either sulfur or nitrogen — it is an ambidentate ligand. Organic thiocyanates[edit] Organic and transition metal derivatives of the thiocyanate ion can exist as "linkage isomers. " Test for iron(III)[edit] References[edit] 4903.full. Rhodanese. Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN-) by converting it to thiocyanate (SCN-).[1] This reaction takes place in two steps. The diagram on the right shows the crystallographically-determined structure of rhodanese. In the first step, thiosulfate reacts with the thiol group on Cysteine-247 1, to form a disulfide 2.

In the second step, the disulfide reacts with cyanide to produce thiocyanate, itself being converted back into the "normal" thiol 1. This reaction is important for the treatment of exposure to cyanide, since the thiocyanate formed is less toxic. Rhodanese shares evolutionary relationship with a large family of proteins, including Rhodanese has an internal duplication. Human proteins containing this domain[edit] References[edit] Jump up ^ Cipollone R, Ascenzi P, Tomao P, Imperi F, Visca P (2008). External links[edit] Rhodanese at the US National Library of Medicine Medical Subject Headings (MeSH) The Effect of Thiamine Tetrahydrofurfuryl Disulfide on Operant Learning ... - Judith Irene Hills. Thiosulfate. The structure of the thiosulfate anion Thiosulfate (S2O32−) (IUPAC-recommended spelling; also thiosulphate in British English) is an oxyanion of sulfur.

The prefix thio- indicates that thiosulfate ion is a sulfate ion with one oxygen replaced by a sulfur. Thiosulfate occurs naturally and is produced by certain biochemical processes. It rapidly dechlorinates water and is notable for its use to halt bleaching in the paper-making industry. Thiosulfate is also useful in smelting silver ore, in producing leather goods, and to set dyes in textiles. Sodium thiosulfate, commonly called hypo ("Hyposulfite"), was widely used in photography to fix black and white negatives and prints after the developing stage; modern 'rapid' fixers use ammonium thiosulfate as a fixing salt because it acts three to four times faster.[1] Some bacteria can metabolise thiosulfates.[2] Formation[edit] [edit] S2O32− (aq) + 2 H+ (aq) → SO2 (g) + S (s) + H2O 2 S2O32− (aq) + I2 (aq) → S4O62− (aq) + 2 I− (aq) Nomenclature[edit]

Thiosulfate sulfurtransferase. In enzymology, a thiosulfate sulfurtransferase (EC 2.8.1.1) is an enzyme that catalyzes the chemical reaction thiosulfate + cyanide sulfite + thiocyanate This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is thiosulfate:cyanide sulfurtransferase. Structural studies[edit] As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1BOH, 1BOI, 1DP2, 1E0C, 1H4K, 1H4M, 1ORB, 1RHD, 1RHS, 1UAR, and 2ORA.

References[edit] Sorbo BH; Lagerkvist, Ulf; Pesola, Rainer; Virtanen, Artturi I.; Sörensen, Nils Andreas (1953). 230402A02_Lonsdale_rw. Mechanism of sulfite cytotoxicity in isol... [Chem Biol Interact. 2008. Super Sulfur. By David Blyweiss, M.D. What do garlic, glutathione, N-acetyl cysteine, alpha-lipoic acid and MSM have in common? Sulfur—a compound that helps the body in a variety of ways, from maintaining healthy joints to boosting the immune system. It’s so important that it is found in every cell of the body. Many amino acids (protein building blocks), vitamins, and minerals also contain sulfur.

But, as important as sulfur is to good health, it’s not a topic of hot discussion—and that’s a shame. Sulfur is the third most abundant mineral in the body after calcium and phosphorus. By sheer quantity, sulfur is more important to health than magnesium, zinc, iron, copper, sodium, iodine—and, for that matter, all vitamins. It also helps maintain oxygen balance for proper brain function. The bad news is that you can’t just run out and by a “sulfur supplement.” Alpha-lipoic acid. Biotin. Methylsulfonylmethane. N-acetylcysteine (NAC). Vitamin B1. References: Bauchart-Thevret C. Heinisch BB. Kim LS. Sulforaphane. Sulforaphane is a molecule within the isothiocyanate group of organosulfur compounds.

It exhibits anticancer and antimicrobial properties in experimental models. It is obtained from cruciferous vegetables such as broccoli, Brussels sprouts or cabbages. It is produced when the enzyme myrosinase transforms glucoraphanin, a glucosinolate, into sulforaphane upon damage to the plant (such as from chewing), which allows the two compounds to mix and react. Young sprouts of broccoli and cauliflower are particularly rich in glucoraphanin. Occurrence and isolation[edit] Sulforaphane was identified in broccoli sprouts, which, of the cruciferous vegetables, have the highest concentration of sulforaphane.[1] It is also found in Brussels sprouts, cabbage, cauliflower, bok choy, kale, collards, Chinese broccoli, broccoli raab, kohlrabi, mustard, turnip, radish, arugula, and watercress. Possible medicinal properties[edit] In vitro studies[edit] Clinical trials[edit] See also[edit] Raphanin References[edit]

Proteomic analysis of covalent modifications of tubul... [J Nutr. 2012. Effect of organosulfur compounds ... [Drug Metabol Drug Interact. 2000. The time-dependent effect of... [J Anim Physiol Anim Nutr (Berl). 2005. Electrophiles in foods: the curren... [Biosci Biotechnol Biochem. 2010. Quantitation of hum... [Cancer Epidemiol Biomarkers Prev. 1992 Jul-Aug.

Glutathione. Thiol groups are reducing agents, existing at a concentration of approximately 5 mM in animal cells. Glutathione reduces disulfide bonds formed within cytoplasmic proteins to cysteines by serving as an electron donor. In the process, glutathione is converted to its oxidized form, glutathione disulfide (GSSG), also called L-(–)-glutathione. Once oxidized, glutathione can be reduced back by glutathione reductase, using NADPH as an electron donor.[3] The ratio of reduced glutathione to oxidized glutathione within cells is often used as a measure of cellular toxicity.[4] Biosynthesis[edit] Glutathione is not an essential nutrient, since it can be synthesized in the body from the amino acids L-cysteine, L-glutamic acid, and glycine. The sulfhydryl (thiol) group (SH) of cysteine serves as a proton donor and is responsible for the biological activity of glutathione.

Cells make glutathione in two adenosine triphosphate (ATP)-dependent steps: Function[edit] Glutathione has multiple functions: Acetylcysteine. Acetylcysteine rINN /əˌsɛtəlˈsɪstiːn/, also known as N-acetylcysteine or N-acetyl-L-cysteine (abbreviated NAC), is a pharmaceutical drug and nutritional supplement used primarily as a mucolytic agent and in the management of paracetamol (acetaminophen) overdose. Other uses include sulfate repletion in conditions, such as autism, where cysteine and related sulfur amino acids may be depleted.[7] Acetylcysteine is a derivative of cysteine; an acetyl group that is attached to the nitrogen atom. This compound is sold as a dietary supplement commonly claiming antioxidant and liver protecting effects.

It is used as a cough medicine because it breaks disulfide bonds in mucus and liquefies it, making it easier to cough up. It is also this action of breaking disulfide bonds that makes it useful in thinning the abnormally thick mucus in cystic and pulmonary fibrosis patients. Medical uses[edit] Paracetamol overdose[edit] Mucolytic therapy[edit] Nephroprotective agent[edit] Microbiological use[edit]

Sulphur