Enhanced peroxidase activity of hemoglobin in a DNA membrane and its application to an unmediated hydrogen peroxide biosensor.

Hemoglobin can exhibit not only a direct electron transfer reacting after being entrapped in a DNA membrane, but also a greatly enhanced peroxidase activity toward the reduction of hydrogen peroxide. Based on the direct electrochemical property and nice enzymatic activity of the protein in a DNA membrane, a reagentless hydrogen peroxide biosensor was prepared. The peak current related to hydrogen peroxide was linearly proportional to its concentration in the range of 1.9 x 10(-6)-6.8 x 10(-4) mol L(-1). The detection limit was 1 x 10(-6) mol/L.

[1]  P. Witting,et al.  The peroxidase activity of a hemin--DNA oligonucleotide complex: free radical damage to specific guanine bases of the DNA. , 2001, Journal of the American Chemical Society.

[2]  James F. Rusling,et al.  Electron Transfer between Electrodes and Heme Proteins in Protein−DNA Films , 1996 .

[3]  A. Santroni,et al.  Antioxidant activities of different hemoglobin derivatives. , 1998, Biochemical and biophysical research communications.

[4]  D. Chinnapen,et al.  Hemin-stimulated docking of cytochrome c to a hemin-DNA aptamer complex. , 2002, Biochemistry.

[5]  R. Baldwin,et al.  Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue. , 1988, Analytical chemistry.

[6]  Akio Fujita,et al.  ENHANCED N-DEMETHYLASE ACTIVITY OF CYTOCHROME C BOUND TO A PHOSPHATE-BEARING SYNTHETIC BILAYER MEMBRANE , 1994 .

[7]  James F. Rusling,et al.  Films of hemoglobin and didodecyldimethylammonium bromide with enhanced electron transfer rates , 1997 .

[8]  Genxi Li,et al.  A reagentless nitric oxide biosensor based on hemoglobin-DNA films , 2000 .

[9]  Fraser A. Armstrong,et al.  Reaction of complex metalloproteins studied by protein-film voltammetry , 1997 .

[10]  D Blohm,et al.  Self-assembly of DNA-streptavidin nanostructures and their use as reagents in immuno-PCR. , 1999, Nucleic acids research.

[11]  P. Bianco,et al.  Electrochemistry of ferredoxin and c-type cytochromes at surfactant film-modified pyrolytic graphite electrodes , 1997 .

[12]  Genxi Li,et al.  Direct Electrochemistry and Enhanced Catalytic Activity for Hemoglobin in a Sodium Montmorillonite Film , 2000 .

[13]  W. Mäntele,et al.  Redox-induced conformational changes in myoglobin and hemoglobin: electrochemistry and ultraviolet-visible and Fourier transform infrared difference spectroscopy at surface-modified gold electrodes in an ultra-thin-layer spectroelectrochemical cell. , 1992, Biochemistry.

[14]  E. Stellwagen.  Haem exposure as the determinate of oxidation–reduction potential of haem proteins , 1978, Nature.

[15]  Genxi Li,et al.  Fabrication of Ultrathin, Protein-containing Films by Layer-by-Layer Assembly and Electrochemical Characterization of Hemoglobin Entrapped in the Film , 2003 .

[16]  T. Kunitake,et al.  Protein Engineering Using Molecular Assembly: Functional Conversion of Cytochrome c via Noncovalent Interactions , 1997 .