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  • Reactivity of the horseradish peroxidase compounds I and II toward organometallic substrates. A stopped-flow kinetic study of oxidation of ferrocenes.

Reactivity of the horseradish peroxidase compounds I and II toward organometallic substrates. A stopped-flow kinetic study of oxidation of ferrocenes.

Biochemistry and molecular biology international (1998-06-23)
V N Goral, A D Ryabov
ANOTACE

Reactivity of horseradish peroxidase compounds I and II (HRP-I and HRP-II) toward organometallicic substrates, viz water-soluble ferrocenes RFc (R = COOH and CH2NMe2), has been studied at 25 degrees C, pH 6.0 and ionic strength 0.1 M. The second-order rate constants k2 for the reaction of HRP-I with FcCOOH and FcCH2NMe2 equal (1.00 +/- 0.04) x 10(6) and (0.27 +/- 0.01) x 10(6) M-1 s-1, respectively. The values of k3 for the reaction of HRP-II with FcCOOH and FcCH2NMe2 equal (1.1 +/- 0.1) x 10(4) and (0.25 +/- 0.01) x 10(4) M-1 s-1, respectively. The steady-state kinetic study of the HRP-catalyzed oxidation of the ferrocenes by H2O2 under the same conditions gave the second-order rate constants of (0.94 +/- 0.03) x 10(4) and (0.24 +/- 0.06) x 10(4) M-1 s-1 for FcCOOH and FcCH2NMe2, respectively, which are in a good agreement with k3. The results reported here confirm the proposal that the rate-limiting step of the steady-state oxidation of ferrocenes is the electron transfer from the substrate to HRP-II.

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Sigma-Aldrich
(Dimethylaminomethyl)ferrocene, ≥95%