Hemoglobin (Hb) was incorporated in dimethylaminoethyl methacrylate (DMAEMA) to form a film and the film was modified on pyrolytic graphite (PG) electrode. UV-Vis spectra suggested that Hb in the film could keep its secondary structure. Consequently, a pair of stable, well-defined, and quasi-reversible cyclic voltammetric peaks could be observed with the formal potential at -206 mV (vs. saturated calomel electrode), characteristic of heme Fe(III)/Fe(II) redox couple of the protein. The apparent heterogeneous electron transfer rate constant and other electrochemical parameters were presented. The catalytic activity of Hb in DMAEMA films toward hydrogen peroxide was also investigated.
direct electrochemistry; hemoglobin; dimethylaminoethyl methacrylate; electrocatalysis
