Direct electrochemistry and electrochemical catalysis of myoglobin-TiO2 coated multiwalled carbon nanotubes modified electrode

Bioelectrochemistry

Volumn 74, Issue 1, 2008, Pages 157-163

  Zhang, Lei ^a   Tian, Dan Bi ^a   Zhu, Jun Jie ^b  

^a NANJING TECH UNIVERSITY   (China)

^b NANJING UNIVERSITY   (China)

Author keywords

Electrocatalysis; Electrochemistry; Multiwalled carbon nanotubes; Myoglobin; TiO2

Indexed keywords

BIOCOMPATIBILITY; CARBON; CARBON NANOTUBES; CATALYSIS; CHEMISTRY; ELECTROCATALYSIS; ELECTROCHEMISTRY; ELECTRODES; ELECTROLYSIS; ELECTRON TRANSITIONS; GLASS MEMBRANE ELECTRODES; HYDROGEN; HYDROGEN PEROXIDE; NANOCOMPOSITES; NANOSTRUCTURED MATERIALS; NANOSTRUCTURES; NANOTUBES; NITRIC OXIDE; OXIDATION; PROTON TRANSFER; REDUCTION; SENSOR NETWORKS;

AMPEROMETRIC DETERMINATIONS; AMPEROMETRIC RESPONSES; ANALYTICAL PERFORMANCES; CATALYTIC ACTIVITIES; DIRECT ELECTROCHEMISTRIES; ELECTROCATALYTIC REDUCTIONS; ELECTROCHEMICAL CATALYSIS; ELECTRODE SURFACES; ELECTRON TRANSFERS; FORMAL POTENTIALS; GC ELECTRODES; GLASSY CARBON ELECTRODES; HYDROGEN PEROXIDE REDUCTIONS; HYDROTHERMAL DEPOSITIONS; LONG TERMS; MODIFIED ELECTRODES; MODIFIED GLASSY CARBON ELECTRODES; MWCNTS FILMS; MYOGLOBIN; NITRIC OXIDE REDUCTIONS; PROMISING MATERIALS; PROTON TRANSPORTATIONS; REVERSIBLE CYCLES; TIO2; VOLTAMMETRIC PEAKS;

MULTIWALLED CARBON NANOTUBES (MWCN);

CARBON; HYDROGEN PEROXIDE; METAL NANOPARTICLE; MULTI WALLED NANOTUBE; MYOGLOBIN; NANOCOMPOSITE; NITRIC OXIDE; TITANIUM DIOXIDE;

AMPEROMETRY; ARTICLE; BIOSENSOR; CATALYSIS; ELECTROCHEMISTRY; ELECTRODE; ELECTRON TRANSPORT; MATERIAL COATING; MICHAELIS CONSTANT; PH; POTENTIOMETRY; PROTON TRANSPORT; REDUCTION;

BIOSENSING TECHNIQUES; CATALYSIS; ELECTROCHEMISTRY; ELECTRODES; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; KINETICS; MYOGLOBIN; NANOPARTICLES; NANOTUBES, CARBON; NITRIC OXIDE; OXIDATION-REDUCTION; TITANIUM;

EID: 54949086304     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2008.07.003     Document Type: Article

References (36)

1. Stellwagen E. Haem exposure as the determinate of oxidation-reduction potential of haem proteins. Nature 275 (1978) 73-74
2. Lin R., Bayachou M., Greaves J., and Farmer P.J. Nitrite reduction by myoglobin in surfactant films. J. Am. Chem. Soc. 119 (1997) 12689-12690
3. Hu N., and Rusling J.F. Electrochemistry and catalysis with myoglobin in hydrated poly(ester sulfonic acid) ionomer films. Langmuir 13 (1997) 4119-4125
4. Bayachou M., Lin R., Cho W., and Farmer P.J. Electrochemical reduction of NO by myoglobin in surfactant film: characterization and reactivity of the nitroxyl (NO-) adduct. J. Am. Chem. Soc. 120 (1998) 9888-9893
5. Immoos C.E., Chou J., Bayachou M., Blair E., Greaves J., and Farmer P.J. Electrocatalytic reductions of nitrite, nitric oxide, and nitrous oxide by thermophilic cytochrome P450 CYP119 in film-modified electrodes and an analytical comparison of its catalytic activities with myoglobin. J. Am. Chem. Soc. 126 (2004) 4934-4942
6. Kawahara N.Y., Ohkubo W., and Ohno H. Effect of cast solvent on the electron transfer reaction for poly(ethylene oxide)-modified myoglobin on the electrode in poly(ethylene oxide) oligomers. Bioconjug. Chem. 8 (1997) 244-248
7. Lvov Y.M., Lu Z., Schenkman J.B., Zu X., and Rusling J.F. Direct electrochemistry of myoglobin and cytochrome P450cam in alternate layer-by-layer films with DNA and other polyions. J. Am. Chem. Soc. 120 (1998) 4073-4080
8. Van Dyke B.R., Saltman P., and Armstrong F.A. Control of myoglobin electron-transfer rates by the distal (nonbound) histidine residue. J. Am. Chem. Soc. 118 (1996) 3490-3492
9. Besteman K., Lee J.O., Wiertz F.G.M., Heering H.A., and Dekker C. Enzyme-coated carbon nanotubes as single-molecule biosensors. Nano Lett. 3 (2003) 727-730
10. 2 nanoparticle films on pyrolytic graphite electrodes: direct electrochemistry and bioelectrocatalysis. Electrochim. Acta 49 (2004) 1981-1988
11. Liu A.H., Wei M.D., Honma I., and Zhou H.S. Direct electrochemistry of myoglobin in titanate nanotubes film. Anal. Chem. 77 (2005) 8068-8074
12. Fan W., and Gao L. Silica nanobeads-decorated multi-walled carbon nanotubes by vapor-phase method. Chem. Lett. 34 (2005) 954-955
13. H.S., and Byler D.M. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
14. Surewicz W.K., and Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 952 (1988) 115-130
15. Koening J.K., and Tabb D.L. Analytical Applications of FTIR to Molecular and Biological Systems (1980), Reidel, Boston MA 241
16. Sarver R.W., and Krueger W.C. An infrared and circular dichroism combined approach to the analysis of protein secondary structure. Anal. Biochem. 199 (1991) 61-67
17. Rusling J.F., and Kumosinski T.F. New advances in computer modeling of chemical and biochemical data. Intell. Instrum. Comput. 10 (1992) 139-145
18. Dong A., Huang P., and Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29 (1990) 3303-3308
19. Dong A., Huang P., and Caughey W.S. Redox-dependent changes in β-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra. Biochemistry 31 (1992) 182-189
20. Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38 (1986) 364
21. Kuznetsova A., Mawhinney D.B., Naumenko V., Yates J.T., Liu J., and Smalley R.E. Enhancement of adsorption inside of single-walled nanotubes: opening the entry ports. Chem. Phys. Lett. 321 (2000) 292-296
22. Mawhinney D.B., Naumenko V., Kuznetsova A., Yates J.T., Liu J., and Smalley R.E. Infrared spectral evidence for the etching of carbon nanotubes: ozone oxidation at 298 K. J. Am. Chem. Soc. 122 (2000) 2383-2384
23. Liu A.H., Wei M.D., Honma I., and Zhou H.S. Direct electrochemistry of myoglobin in titanate nanotubes film. Anal. Chem. 77 (2005) 8068-8074
24. Luo H., Shi Z., Li N., Gu Z., and Zhuang Q. Investigation of the electrochemical and electrocatalytic behavior of single-wall carbon nanotube film on a glassy carbon electrode. Anal. Chem. 73 (2001) 915-920
25. Luo H.X., Shi Z.J., Li N.Q., Gu Z.N., and Zhuang Q.K. Investigation on the electrochemical and electrocatalytic behavior of chemically modified electrode of single wall carbon nanotube functionalized with carboxylic acid group. Chem. J. Chin. Univ. 21 (2000) 1372-1374
26. 2. Biosens. Bioelectron. 22 (2007) 899-904
27. Liu H.H., Tian Z.Q., Lu Z.X., Zhang Z.L., Zhang M., and Pang D.W. Direct electrochemistry and electrocatalysis of heme-proteins entrapped in agarose hydrogel films. Biosens. Bioelectron. 20 (2004) 294-304
28. Liu H.H., Wan H.Q., and Zou G.L. Direct electrochemistry and electrochemical catalysis of immobilized hemoglobin in an ethanol-water mixture. Anal. Bioanal. Chem. 385 (2006) 1470-1476
29. Xu Q., Mao C., Liu N.N., Zhu J.J., and Sheng J. Direct electrochemistry of horseradish peroxidase based on biocompatible carboxymethyl chitosan-gold nanoparticle nanocomposite. Biosens. Bioelectron. 22 (2006) 768-773
30. Laviron E. General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems. J. Electroanal. Chem. 101 (1979) 19-28
31. Nassar A.E.F., Zhang Z., Hu N., Rusling J.F., and Kumosinski T.F. Proton-coupled electron transfer from electrodes to myoglobin in ordered biomembrane-like films. J. Phys. Chem. B 101 (1997) 2224-2231
32. Huang H., He P., Hu N., and Zeng Y. Electrochemical and electrocatalytic properties of myoglobin and hemoglobin incorporated in carboxymethyl cellulose films. Bioelectrochemistry 61 (2003) 29-38
33. Kamin R.A., and Wilson G.S. Rotating ring-disk enzyme electrode for biocatalysis kinetic studies and characterization of the immobilized enzyme layer. Anal. Chem. 52 (1980) 1198-1205
34. Shang L.B., Liu X.J., Zhong J., Fan C.H., Suzuki I., and Li G.X. Fabrication of ultrathin, protein-containing films by layer-by-layer assembly and electrochemical characterization of hemoglobin entrapped in the film. Chem. Lett. 32 (2003) 296
35. Fan C.H., Li G.X., Zhu J.Q., and Zhu D.X. A reagentless nitric oxide biosensor based on hemoglobin-DNA films. Anal. Chim. Acta 423 (2000) 95-100
36. Fan C.H., Pang J.T., Shen P.P., Li G.X., and Zhu D.X. Nitric oxide biosensors based on Hb/phosphatidylcholinefilms. Anal. Sci. 18 (2002) 129-132