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Interaction of aromatic donor molecules with horseradish peroxidase: identification of the binding site and role of heme iron in the binding and activity

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Abstract

The interaction of aromatic substrates with horseradish peroxidase (HRP) was studied. Chemical modification of HRP was performed using diethylpyrocarbonate (DEPC) and for the first time the amino acid involved in binding with these substrates has been identified. The kinetic parameters for this interaction have been calculated and the role of heme iron in the oxidation of aromatic substrates by HRP has been discussed.

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  1. Biological NMR Centre, Medical Science Building, University of Leicester, Leicester, UK

    Sandeep Modi

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  1. Sandeep Modi
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Modi, S. Interaction of aromatic donor molecules with horseradish peroxidase: identification of the binding site and role of heme iron in the binding and activity. Biometals 8, 218–222 (1995). https://doi.org/10.1007/BF00143379

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  • DOI: https://doi.org/10.1007/BF00143379

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