Direct electrochemistry behavior of Cytochrome c on silicon dioxide nanoparticles-modified electrode

A newfangled direct electrochemistry behavior of Cytochrome c (Cyt c) was found on glassy carbon (GC) electrode modified with the silicon dioxide (SiO2) nanoparticles by physical adsorption. A pair of stable and well-defined redox peaks of Cyt c ' quasi-reversible electrochemical reaction were obtained with a heterogeneous electron transfer rate constant of 1.66 x 10(-3) cm/s and a formal potential of 0.069 V (vs. Ag/AgCl) (0.263 V versus NHE) in 0.1 mol/L pH 6.8 PBS. Both the size and the amount of SiO2 nanoparticles could influence the electron transfer between Cyt c and the electrode. Electrostatic interaction which is between the negative nanoparticle surface and positively charged amino acid residues on the Cyt c surface is of importance for the stability and reproducibility toward the direct electron transfer of Cyt c. It is suggested that the modification of SiO2 nanoparticles proposes a novel approach to realize the direct electrochemistry of proteins.

Polyelectrolyte-functionalized ionic liquid for electrochemistry in supporting electrolyte-free aqueous solutions and application in amperometric flow injection analysis

As a green process, electrochemistry in aqueous solution without a supporting electrolyte has been described based on a simple polyelectrolyte-functionalized ionic liquid (PFIL)-modified electrode. The studied PFIL material combines features of ionic liquids and traditional polyelectrolytes. The ionic liquid part provides a high ionic conductivity and affinity to many different compounds. The polyelectrolyte part has a good stability in aqueous solution and a capability of being immobilized on different substrates. The electrochemical properties of such a PFIL-modified electrode assembly in a supporting electrolyte-free solution have been investigated by using an electrically neutral electroactive species, hydroquinone ( HQ) as the model compound. The partition coefficient and diffusion coefficient of HQ in the PFIL film were calculated to be 0.346 and 4.74 X 10(-6) cm(2) s(-1), respectively. Electrochemistry in PFIL is similar to electrochemistry in a solution of traditional supporting electrolytes, except that the electrochemical reaction takes place in a thin film on the surface of the electrode. PFILs are easily immobilized on solid substrates, are inexpensive and electrochemically stable. A PFIL-modified electrode assembly is successfully used in the flow analysis of HQ by amperometric detection in solution without a supporting electrolyte.

Electrochemistry and electrogenerated chemiluminescence of SiO2 nanoparticles/tris(2,2 '-bipyridyl)ruthenium(II) multilayer films on indium tin oxide electrodes

In this paper, a simple method of preparing {SiO2/Ru-(bPY)(3)(2+)}(n) multilayer films was described. Positively charged tris(2,2'-bipyridyl)ruthenium(II) (Ru(bpy)(3)(2+)) and negatively charged SiO2 nanoparticles were assembled on ITO electrodes by a layer-by-layer method. Electrochemical and electrogenerated chemiluminescence (ECL) behaviors of the {SiO2/Ru(bpy)(3)(2+)}(n) multilayer film-modified electrodes were studied. Cyclic voltammetry, UV-visible spectroscopy, quartz crystal microbalance, and ECL were adopted to monitor the regular growth of the multilayer films. The multilayer films containing Ru(bpy)(3)(2+) was used for ECL determination of TPA, and the sensitivity was more than 1 order of magnitude higher than that observed for previous reported immobilization methods for the determination of TPA. The multilayer films also showed better stability for one month at least. The high sensitivity and stability mainly resulted from the high surface area and special structure of the silica nanoparticles.

Direct electrochemistry and bioelectrocatalysis of horseradish peroxidase immobilized on active carbon

For the first time horseradish peroxidase (HRP) immobilized on the surface of active carbon powder modified at the surface of a glassy carbon electrode has been shown to undergo a direct quasi-reversible electrochemical reaction. Its formal potential, E-o/, is -0.363 V in phosphate buffer solution (pH 6.8) at a scan rate of 100 mV/s and is almost independent of the scan rate in the range of 50-700 mV/s. The dependence of E-o/ on the pH of the buffer solution indicated that the conversion of HRP-Fe(III)/HRP-Fe(II) is a one-electron-transfer reaction process coupled with one-proton-transfer. The experimental results also demonstrated that the immobilized HRP retained its bioelectrocatalytic activity to the reduction of H2O2. Furthermore, the HRP adsorbed oil the surface of the active carbon powder can be stored at 4 degreesC for several months without any loss of the enzyme activity. The method presented for immobilizing HRP can be easily extended to immobilize and obtain the direct electrochemistry of other enzymes.

Interaction of echinomycin with guanine: electrochemistry and spectroscopy studies

The interaction of antitumor antibiotic, echinomycin (Echi) with guanine (Gua) was thoroughly investigated by adsorptive transfer stripping cyclic voltammetry, ultraviolet and visible adsorption spectra (UV/Vis) and Fourier-transform infrared spectroscopy (FTIR). Electrochemistry provided a simple tool for verifying the occurrence of interaction between Echi and Gua. Echi could be accumulated from the solution and give well-defined electrochemical signals in 0.1 M phosphate buffer solution (pH 7.0) only when Gua was present on the surface of the electrochemically pretreated glass carbon electrode (GCE), suggesting a strong binding of Echi to Gua. All the acquired spectral data showed that a new adduct between Echi and Gua was formed, and two pairs of adjacent intermolecular hydrogen bonds between the Ala backbone atoms in Echi and Gua (Ala-NH to Gua-N3 and Gua-NH2 to Ala-CO) played a dominating role in the interaction. Electrochemistry coupled with spectroscopy techniques could provide a relatively easy way to obtain useful insights into the molecular mechanism of drug-DNA interactions, which should be important in the development of new anticancer drugs with specific base recognition.

Immobilization and direct electrochemistry of copper-containing enzymes on active carbon

Two typical and important copper-containing enzymes, laccase (Lac) and tyrosinase (Tyr), have been immobilized on the surface of active carbon with simple adsorption method. The cyclic voltammetric results indicated that the active carbon could promote the direct electron transfer of both Lac and Tyr and a pair of well-defined and nearly symmetric redox peaks appeared on the cyclic voltammograms of Lac or Tyr with the formal potential, E-0', independent on the scan rate. The further experimental results showed that the immobilized copper-containing oxidase displayed an excellent electrocatalytic activity to the electrochemical reduction of O-2. The immobilization method presented here has several advantages, such as simplicity, easy to operation and keeping good activity of enzyme etc., and could be further used to study the direct electrochemistry of other redox proteins and enzymes and fabricate the catalysts for biofuel cell.