Direct electron transfer of hemoglobin founded on electron tunneling of CTAB monolayer.

Direct electron transfer and stable adsorption of hemoglobin (Hb) on a carbon paste (CP) electrode were achieved with the aid of a single-chain cationic surfactant, namely, cetyltrimethylammonium bromide (CTAB). Cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS) indicated that CTAB could form a complete monolayer with a high density of positive charges on the surface of the CP electrode, which strongly adsorbed negatively charged protein molecules via electrostatic interactions. The surfactant molecules anchored the protein molecules to align in suitable orientations and acted as electron-tunneling pathways between the protein molecules and the CP electrode. The bioelectrocatalytic activity of the immobilized Hb was confirmed by RAIR and UV-vis spectroscopies, and rapid electrochemical responses to the reduction of oxygen (O2), hydrogen peroxide (H2O2), and nitrite (NO2-) were also obtained.