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Reactions of radiolytically generated CO 3 •-with some ferric heme proteins, catalase, cytochrome c, and horseradish peroxidase (HRP), were studied. Carbonate radical anion oxidized amino acid residues of these proteins, but did not react directly with heme iron. HRP and catalase lost about 30% and 20% of their activity, respectively, after the reaction with 100 lM of CO 3•-. The rate constants of the reactions of CO 3•-with the investigated proteins measured by the pulse radiolysis method at pH 8-8.4 and 10 varied from 1.0 9 10 8 M -1 s -1 (for cytochrome c) to 3.7 9 10 9 M -1 s -1 (for catalase).