Electrochemical investigation of immobilized hemoglobin: redox chemistry and enzymatic catalysis.
Hb entrapped in the Konjak glucomannan (KGM) film could transfer electrons directly to an edge-plane pyrolytic graphite (EPG) electrode, corresponding to the redox couple of Fe(III)/Fe(II). The redox properties of Hb, such as formal potential, electron transfer rate constant, the stability of the redox state of protein and redox Bohr effect, were characterized by cyclic voltammetry and square wave voltammetry. The stable Hb-KGM/EPG gave analytically useful electrochemical catalytic responses to oxygen, hydrogen peroxide and nitrite.
Liu
Hui-Hong
HH
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China. liuhh@xfu.edu.cn
Zou
Guo-Lin
GL
D000818:Animals; D015374:Biosensing Techniques; D002384:Catalysis; D002417:Cattle; D004563:Electrochemistry / Q000379:methods; D004566:Electrodes; D006454:Hemoglobins / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D009573:Nitrites / Q000032:analysis*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000032:analysis*
D006454:Hemoglobins; D009573:Nitrites; D007501:Iron; D010100:Oxygen