Formation of horseradish peroxidase compound 1 with alkyl hydroperoxides
1979
Paul, K.G. | Ohlsson, P.I. | Wold, S. (Umeaa Univ. (Sweden). Dept. of Chemistry)
The rates of formation of compound I from the acidic isoenzyme horseradish peroxidase A2 and the hydrogen, methyl, ethyl, propyl, butyl, isopropyl, tert-butyl and cumenyl hydroperoxides have been determined. The rate constants, K(,1)(, app), have been related to other properties of the peroxides: Acidity, dissociation energy of the RO-OH bond, rate of diffusion (of the corresponding alcohol ROH), van der Waals volumes and the substituent parameters MR, ES, pi, L and B(,1) (molecular refractivity, Taft's steric, Hansch's lipophilic, Verloop's length and width parameters, respectively). A fair correlation was found between log k(,1)(, app) and pK(, a). Steric effects (ES) contribute and account for the difference between the n-alkyl homologues.
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