Direct electrochemistry and electrocatalysis of hemoglobin at three-dimensional gold film electrode modified with self-assembled monolayers of 3-mercaptopropylphosphonic acid

Multilayered hemoglobin (Hb) molecules Were successfully immobilized oil three-dimensional gold film electrode modified with self-assembled monolayers (SAMs) of 3-mercaptopropylphosphonic acid. Direct electrochemistry of the immobilized multilayered Hb Occurs with high thermal stability and electrochemical stability. In the multilayered Hb film, the most inner HI) molecules call directly transfer electron with the electrode, while the M protein beyond this layer communicates electron with the electrode via protein-protein electron exchange. In addition, the proposed functional interface call greatly enhance electron transfer rate of the immobilized Hb protein (k(s) = 15.8 +/- 2.0 s(-1)) clue to the increase Of roughness of the gold substrate. Under optimized experimental conditions, the multilayered Hb film displays good bioelectrocatalytic activity toward the reduction of hydrogen peroxide. This electrochemical sensor shows fast response (less than 1 s), wide linear range (7.8 x 10(-8) to 9.1 x 10(-5) M) and low detection limit (2.5 x 10(-8) M), which call be attributed to good mass transport. large Hb proteins loading per unit area and fast electron transfer rate of Hb protein. (C) 2009 Elsevier B.V. All rights reserved.