2.02012-07-30 14:55:01 -06002015-06-03 17:20:57 -0600ECMDB21231M2MDB001639Hydrogen cyanideHCN is formed in interstellar clouds through one of two major pathways: via a neutral-neutral reaction (CH2 + N <=> HCN + H) and via dissociative recombination (HCNH+ + e- <=> HCN + H). The dissociative recombination pathway is dominant by 30%; however, the HCNH+ must be in its linear form. Dissociative recombination with its structural isomer, H2NC+ produces hydrogen isocyanide (HNC), exclusively.; HCN is produced on an industrial scale and is a highly valuable precursor to many chemical compounds ranging from polymers to pharmaceuticals.; Hydrogen cyanide (with the historical common name of Prussic acid) is an inorganic compound with chemical formula HCN. It is a colorless, extremely poisonous liquid that boils slightly above room temperature at 26 ACAcide cyanhydriqueAcido cianidricoAero Liquid HCNAgent ACBlausaeureBlausaeure (German)BlausaureBlauwzuurCarbon hydride nitrideCarbon hydride nitride (CHN)Cn-, cyanoCyaanwaterstofCyanideCyanwasserstoffCyclonCyclone BCyjanowodorEvercynFormic anammonideFormonitrileHCNHydridonitridocarbonHydrocyanateHydrocyanic acidHydrogen cyanideHydrogen(nitridocarbonate)Hydrogen(nitridocarbonic acid)MethanenitrileNitrilomethanePrussatePrussate, unstabilizedPrussic AcidPrussic acid, unstabilizedZaclondiscoidsZootateZootic acid[CHN]CHN27.025327.010899037formonitrilehydrogen cyanide74-90-8C#NInChI=1S/CHN/c1-2/h1HLELOWRISYMNNSU-UHFFFAOYSA-NLiquidCytosolExtra-organismPeriplasmlogp-0.65logs-0.92solubility3.26e+00 g/lmelting_point-13.4 oClogp-0.35pka_strongest_acidic9.5iupacformonitrileaverage_mass27.0253mono_mass27.010899037smilesC#NformulaCHNinchiInChI=1S/CHN/c1-2/h1HinchikeyLELOWRISYMNNSU-UHFFFAOYSA-Npolar_surface_area23.79refractivity7.01polarizability2.31rotatable_bond_count0acceptor_count1donor_count0physiological_charge0formal_charge0Thiosulfate Disproportionation IIIThiosulfate sulfurtransferase is more often referred to by the name rhodanese, from the German word for thiocyanate, "rhodanid". The enzyme catalyzes the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. The original description of rhodanese, purified from bovine mitochondria, used thiosulfate and cyanide for this purpose. Rhodanese is a widespread enzyme, and has been detected in many major phyla, both prokaryotic and eukaryotic. Despite its ubiquity, the physiological role of rhodanese has not yet been established unambiguously. It has been suggested that rhodanese is involved in detoxification of cyanide in both mammals and bacteria. It has also been proposed that rhodanese, using the dithiol dihydrolipoate as the sulfur acceptor, may act as a sulfur insertase involved in the formation of prosthetic groups in iron-sulfur proteins, such as ferredoxin. (EcoCyc)PW002060Metabolicthiosulfate disproportionation III (rhodanese)PWY-5350Specdb::CMs34474Specdb::CMs172526Specdb::EiMs342Specdb::NmrOneD2604Specdb::NmrOneD56882Specdb::NmrOneD56883Specdb::NmrOneD56884Specdb::NmrOneD56885Specdb::NmrOneD56886Specdb::NmrOneD56887Specdb::NmrOneD56888Specdb::NmrOneD56889Specdb::NmrOneD56890Specdb::NmrOneD56891Specdb::MsMs9368Specdb::MsMs9369Specdb::MsMs9370Specdb::MsMs16040Specdb::MsMs16041Specdb::MsMs16042768748C0132618407HCNCYNHydrogen_cyanideKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Thiosulfate sulfurtransferase glpEP0A6V5GLPE_ECOLIglpEhttp://ecmdb.ca/proteins/P0A6V5.xml3-mercaptopyruvate sulfurtransferaseP31142THTM_ECOLIsseAhttp://ecmdb.ca/proteins/P31142.xmlThiosulfate sulfurtransferase YnjEP78067YNJE_ECOLIynjEhttp://ecmdb.ca/proteins/P78067.xmlThiosulfate sulfurtransferase PspEP23857PSPE_ECOLIpspEhttp://ecmdb.ca/proteins/P23857.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlHydrogen cyanide + Thiosulfate > Hydrogen ion + Sulfite + ThiocyanateHydrogen cyanide + 3-Mercaptopyruvic acid + Cyanide <> Hydrogen ion + Pyruvic acid + ThiocyanateR03106MERCAPYSTRANS-RXNHydrogen cyanide + 3-Mercaptopyruvic acid <> Thiocyanate + Pyruvic acidR03106MERCAPYSTRANS-RXNHydrogen cyanide + 3-Mercaptopyruvic acid Hydrogen ion + Pyruvic acid + ThiocyanateMERCAPYSTRANS-RXN<i>S</i>-sulfanyl-[acceptor] + Hydrogen cyanide an unsulfurated sulfur acceptor + Thiocyanate + Hydrogen ionRXN0-6359Thiosulfate + Hydrogen cyanide > Sulfite + Thiocyanate3-Mercaptopyruvic acid + Hydrogen cyanide > Pyruvic acid + ThiocyanateHydrogen cyanide + Thiosulfate > Thiocyanate + Sulfite +2 Hydrogen ionPW_R006013