2.0 2012-05-31 10:27:39 -0600 2015-06-03 15:53:31 -0600 ECMDB00598 M2MDB000154 Sulfide Sulfide is an ion form of sulfur, frequently found in hydrogen sulfide. Sulfur (Greek is theion) is the chemical element in the periodic table that has the symbol S and atomic number 16. It is an abundant, tasteless, odorless, multivalent non-metal. Sulfur, in its native form, is a yellow crystalline solid. In nature, it can be found as the pure element or as sulfide and sulfate minerals. It is an essential element for life. The amino acids cysteine and methionine contain sulfur, as do all polypeptides, proteins, and enzymes which contain these amino acids. This makes sulfur a necessary component of all living cells. Disulfide bonds between polypeptides are very important in protein assembly and structure. Homocysteine and taurine are also sulfur containing amino acids but are not coded for by DNA nor are they part of the primary structure of proteins. Some forms of bacteria use hydrogen sulfide (H2S) in the place of water as the electron donor in a primitive photosynthesis-like process. Inorganic sulfur forms a part of iron-sulfur clusters, and sulfur is the bridging ligand in the CuA site of cytochrome c oxidase. Sulfur is an important component of coenzyme A. Sulfanediide Sulfide Sulfide(2-) Sulfur Sulfur(2-) Sulphanediide Sulphide Sulphide(2-) Sulphur Sulphur(2-) S 32.065 31.97207069 sulfanediide sulfanediide 18496-25-8 [S--] InChI=1S/S/q-2 UCKMPCXJQFINFW-UHFFFAOYSA-N Solid Cytoplasm Periplasm melting_point 112 oC logp -0.037 ChemAxon iupac sulfanediide ChemAxon average_mass 32.065 ChemAxon mono_mass 31.97207069 ChemAxon smiles [S--] ChemAxon formula S ChemAxon inchi InChI=1S/S/q-2 ChemAxon inchikey UCKMPCXJQFINFW-UHFFFAOYSA-N ChemAxon polar_surface_area 0 ChemAxon refractivity 5.76 ChemAxon polarizability 2.93 ChemAxon rotatable_bond_count 0 ChemAxon acceptor_count 0 ChemAxon donor_count 0 ChemAxon physiological_charge -1 ChemAxon formal_charge -2 ChemAxon Sulfur metabolism The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. The alkyl sulfate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described. PW000922 ec00920 Metabolic lipoate biosynthesis and incorporation II PWY0-1275 lipoate biosynthesis and incorporation I PWY0-501 Specdb::CMs 102747 Specdb::CMs 102748 Specdb::EiMs 2006 Specdb::NmrOneD 5207 Specdb::MsMs 107859 Specdb::MsMs 107860 Specdb::MsMs 107861 Specdb::MsMs 174948 Specdb::MsMs 174949 Specdb::MsMs 174950 HMDB00598 5362487 27079 C00297 26833 CPD-7046 Sulfur Keseler, I. 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The reactions of sulfur atoms with propadiene and 1,2-butadiene. Canadian Journal of Chemistry (1985), 63(3), 667-75. Sulfite reductase [NADPH] hemoprotein beta-component P17846 CYSI_ECOLI cysI http://ecmdb.ca/proteins/P17846.xml Sulfite reductase [NADPH] flavoprotein alpha-component P38038 CYSJ_ECOLI cysJ http://ecmdb.ca/proteins/P38038.xml Sulfide + Water + 3 NADP > Sulfite +3 NADPH + Sulfite +3 NADPH PW_R003839