Abstract

Efficient quenching of eosin phosphorescence by amino-acid derivatives of fullerene (AADFs) such as C60-alanine and C60-glycine in aqueous solutions indicates the possibility of transferring electrons from eosin to fullerene upon collisions or in the exciplex state. To investigate electron transfer in the protein structure, we studied the process of incorporation of C60-alanine and C60-glycine into the heme pocket of myoglobin by controlling Forster quenching. The dissociation constant for the protein-AADF complex was estimated.

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