Abstract
Reactions of Br2− radical anion with heme enzymes, catalase and horseradish peroxidase, have been studied by pulse radiolysis. It has been found that Br2− does not react with the heme centre of investigated enzymes. Dibromine radical anion reacts with tryptophan residues of catalase without any influence on the activity of catalase. It is suggested that in pulse radiolysis studies, where horseradish peroxidase is at about tenfold excess towards Br2−, the enzyme is modified rather by Br2, than by Br2−.
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