| 7350910 |
Gewitz HS, Piefke J, Langowska K, Vennesland B: The formation of hydrogen cyanide from histidine in the presence of amino acid oxidase and peroxidase. Biochim Biophys Acta. 1980 Jan 11;611(1):11-26.
Conditions were sought to increase the yield of HCN from L-histidine incubated with L-amino acid oxidase (L-amino acid:oxygen oxidoreductase (deaminating), EC 1.4.3.2) from snake venom, and horseradish peroxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7). Small amounts of histidine and high buffer concentrations favored high HCN yields, which reached a maximum of 72%. Imidazole 4-aldehyde and imidazole 4-carboxylic acid were identified among the reaction products, together with CO2, NH3, H2O2 and imidazole acetic acid. The CO2 formed was equal to the histidine oxidized, and to the sum of NH3 plus HCN formed. The production of HCN was associated with an increased O2 uptake, which was established from the beginning of the reaction, with no apparent lag and ranged from 1.2 to 1.6 mumol extra O2 taken up/mumol HCN formed. The system was inhibited by catalase, but added superoxide dismutase caused a small stimulation of both HCN production and O2 consumption, and a larger stimulation of H2O2 accumulation. Added hydroxylamine was cooxidized to nitrite in an amount equimolar with the HCN formed. This nitrite formation was inhibited by superoxide dismutase. The facts could be interpreted in terms of superoxide anion formation during the HCN-producing reaction. cytochrome c, heme, or ferricyanide could be substituted for peroxidase, but were less effective. The initial rates of HCN formation from phenylalanine, tyrosine and tryptophan were higher, but the eventual yields of HCN from these amino acids were lower than those from histidine. |
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