Effect of solvent viscosity, polarity and pH on the charge transfer between tryptophan radical and tyrosine in bovine serum albumin: a pulse radiolysis study

Abstract

The effect of viscosity, solvent polarity and pH of the medium on the reaction of a protein, bovine serum albumin (BSA), with organohalo-peroxyl radical in aqueous solution has been studied using pulse radiolysis technique. Unlike in dilute aqueous solution, electron transfer from tyrosine to tryptophan radical in BSA has been clearly observed at a viscosity of 7.7 centiPoise (cP). The oxidation of BSA, tryptophan and tyrosine in different media has also been compared with those taking place in dilute aqueous solution. The effect of solvent characteristics on the observed charge transfer has been discussed.