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. Organic thiocyanates[edit] Organic and transition metal derivatives of the thiocyanate ion can exist as "linkage isomers. " Phenylthiocyanate and phenylisothiocyanate are linkage isomers and are bonded differently Organic thiocyanates are hydrolyzed to thiocarbamates in the Riemschneider thiocarbamate synthesis. 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. 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. 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.
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. 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.” 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.
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. Cells make glutathione in two adenosine triphosphate (ATP)-dependent steps: First, gamma-glutamylcysteine is synthesized from L-glutamate and cysteine via the enzyme gamma-glutamylcysteine synthetase (glutamate cysteine ligase, GCL).
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]