Reduction of Selected Oligopeptides Containing Methionine Induced by Hydrated Electrons

Abstract

Bimolecular rate constants for the reaction of the hydrated electron with zwitterionic forms of several linear oligopeptides containing methionine were determined using the pulse radiolysis technique. The rate constants were found to vary in the range of (0.2-1.2) x 10(9) M(-1) s(-1). The reactivity of the peptides toward e(aq)- is governed by the pKa of the N-terminal amino group and the number of peptide bonds. At a fixed number of peptide bonds, the reactivity increases with the pKa, and for a given N-terminal amino acid residue, it increases with the number of peptide bonds. For the linear peptides the observed transient spectra are assigned to deaminated oligopeptide radicals, *CHRCONH approximately, obtained due to rapid deamination of the corresponding electron adducts formed initially. The radicals derived from oligopeptides containing methionine at the N-terminus absorb at approximately 400 nm with extinction coefficients of approximately 1300+/-150 M(-1) cm(-1). Their absorption maxima are shifted hypsochromically by approximately 30 nm with respect to those derived from oligopeptides with glycine at the N-terminus. The e(aq)- reacts with cyclic Met-Met, k = 2.0 x 10(9) M(-1) s(-1), probably by addition to the carbonyl bond, forming an adduct absorbing below 250 nm with epsilon250 = 2300+/-250 M(-1) cm(-1).