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- W1998361764 abstract "1. The oxidation of ethanol by a mixture of H2O2 and catalase has been studied. By using a 1.106-fold excess of ethanol (H2A) over H2O2, the competition between ethanol and H2O2 for the active enzyme-substrate complex (CI) has been demonstrated. 2. Under conditions where ethanol competes for CI, the overall second-order rate constant (kH) becomes a function of the ratio of the concentrations of ethanol and H2O2 (R). An increase of R causes a decrease of kH. 3. From the dependence of kH on R the individual rate constants of the peroxidatic mechanism of catalase action have been calculated. E + H2O2→ICIk1 = (5.6 ± 0.5) · IO6M-1 · sec-1CI + H2O2→4E + O2 + 2 H2Ok4 = (I.2 ± 0.I) · IO7M-1 · sec-1CI + H2A→5E + A + 2 H2Ok5 = (I.8 ± 0.4) · IO2M-1 · sec-1 4. From these results a steady-state saturation of 30% of catalase hematins by H2O2 during the catalatic reaction has been calculated." @default.
- W1998361764 created "2016-06-24" @default.
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- W1998361764 date "1970-02-01" @default.
- W1998361764 modified "2023-10-16" @default.
- W1998361764 title "Peroxidatic activity of catalase" @default.
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- W1998361764 doi "https://doi.org/10.1016/0005-2744(70)90052-5" @default.
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