The cofactor hemin modified with aminomethylferrocene was loaded into the apo form of horseradish peroxidase (HRP) to give Fc-HRP (scheme); this reconstituted enzyme is electrochemically and catalytically active with respect to ABTS and water-soluble ferrocenes. The ferrocenes display kinetically meaningful affinity to the reconstituted enzyme owing to creation of a novel artificial hydrophobic binding site at the protein surface.
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Ryabov et al. (1999) studied this question.
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