Horseradish peroxidase. XXXVI. On the difference between peroxidase and metmyoglobin. |
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Authors: | H B Dunford T Araiso |
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Affiliation: | Department of Chemistry, University of Alberta Edmonton, Alberta, Canada T6G 2G2 |
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Abstract: | A mechanism for the reaction of hydrogen peroxide with horseradish peroxidase is proposed which involves the catalytic activity of the carboxylate side chain of aspartate residue 43. The corresponding residue in the active site of metmyoglobin is glycine E8, which explains the inability of metmyoglobin to form compound I. Certain aspects of the proposed peroxidase mechanism may be relevant to the catalytic triad for the serine proteases. |
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