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  • Title: 1-Aminocyclopropane-1-carboxylic acid as a substrate of peroxidase: conditions for oxygen consumption, hydroperoxide generation and ethylene production.
    Author: Acosta M, Casas JL, Arnao MB, Sabater F.
    Journal: Biochim Biophys Acta; 1991 Apr 29; 1077(3):273-80. PubMed ID: 2029526.
    Abstract:
    Conditions in which 1-aminocyclopropane-1-carboxylic acid (ACC) functions as a substrate of peroxidase have been investigated by measuring oxygen consumption in the reaction medium and the production of ethylene. In both cases, the presence of Mn2+ and either H2O2 or the activated form of peroxidase, namely compound I of peroxidase, was found to be essential. Both oxygen consumption and ethylene production were dependent on enzyme concentration, the optimum ACC/Mn2+ ratio being 1:1. Oxygen consumption in a system with ACC, Mn2+ and compound I showed an enzyme-dependent lag phase and then proceeded to total depletion, suggesting that the system itself generates hydroperoxides that completed the catalytic cycle of the enzyme. The presence of these hydroperoxides in the reaction medium was detected by a colorimetric method. High H2O2 concentration progressively decreased oxygen consumption, the same effect being produced by catalase. Ethylene production was oxygen dependent, mediated by ACC-free radicals and gave a poor yield. The results suggest that the fate of these ACC-free radicals determines the yield in ethylene. These radicals must be oxidized immediately, otherwise their stabilization to hydroperoxides would prevent ethylene production.
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