Reactions of heme proteins with carbonate radical anion

Reactions of heme proteins with carbonate radical anion Reactions of radiolytically generated CO3 •− 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 μM of CO3 •−. The rate constants of the reactions of CO3 •− with the investigated proteins measured by the pulse radiolysis method at pH 8–8.4 and 10 varied from 1.0 × 108 M−1 s−1 (for cytochrome c) to 3.7 × 109 M−1 s−1 (for catalase). Research on Chemical Intermediates Springer Journals

Reactions of heme proteins with carbonate radical anion

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Springer Netherlands
Copyright © 2009 by Springer Science+Business Media BV
Chemistry; Inorganic Chemistry ; Physical Chemistry ; Catalysis
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