Surface Study of Lithium-Air Battery Oxygen Cathodes in Different Solvent-Electrolyte pairs.

The O2/Li2O2 electrode reaction has been studied on low surface area Au electrodes in three solvent-electrolyte pairs (0.1 M LiPF6/DMSO, LiPF6/ACN, and LiBF4/ACN) using an electrochemical cell coupled to UHV XPS spectrometer, EQCM, AFM, and DEMS. The XPS spectra of the surfaces after treatment at selected electrode potentials for the O2 reduction and reoxidation of the surface show the presence of C and S from solvent decomposition and of F and P from electrolyte decomposition. Furthermore, Li 1s and O 1s peaks due to Li2O2 and decomposition products such as carbonate, organics, LiF, high oxidation sulfur, and phosphorus compounds were also observed. Using ACN instead of DMSO results in less solvent decomposition, whereas using LiBF4 results in less electrolyte decomposition. XPS, AFM, and EQCM show that O2 reduction products removal only takes place at very high overpotentials. In agreement with XPS which shows removal of carbonate surface species, DEMS confirms evolution of CO2 and consumption of O2 at 4.5 V, but LiF cannot be removed completely in a round trip of the Li-O2 battery cathode.

Selective electrocatalytic hydrogenation using palladium nanoparticles electrochemically formed in layer-by-layer multilayer films.

Sequential adsorption of PdCl4(2-) within weak polyelectrolyte layer-by-layer (LbL) self-assembled multilayer films with further electrochemical reduction to yield Pd(0) nanoparticles (Pd-NPs) has been demonstrated. The electrocatalytic hydrogenation (ECH) of model molecules such as acetophenone and benzophenone on Pd-NPs of different sizes (6 to 35 nm) and bulk Pd crystal surface in hydroalcoholic acid solution has been investigated. Distribution of reaction products (secondary alcohols and alkanes) and faradaic yield was systematically investigated. While the polyelectrolyte multilayers act as nanoreactors by confining PdCl4(2-) ions and preventing the formation of large crystals, their presence also alters the hydrogenation reaction and therefore heat treated surfaces showed only the effect of nanocrystal size on the reaction selectivity and faradaic yield.

Charge regulation in redox active monolayers embedded in proton exchanger surfaces.

Experimental evidence of the variation in redox potential of osmium pyridine complexes tethered to a Au surface by thiol or diazonium chemistry at different ionic concentration and electrolyte pH is described. The interplay between the charged redox and acid groups is described by a charge regulation model based on PM-IRRAS spectroscopic evidence on the different degrees of surface protonation.

Electrochemistry of Os(2,2'-bpy)2ClPyCH2NHCOPh tethered to Au electrodes by S-Au and C-Au junctions.

Osmium pyridine-bipyridine redox centers have been tethered to Au electrodes by chemical modification through Au-S and Au-C bonds respectively. 4-Mercapto benzoic acid and the reduction product of the aryl diazonium salt of 4-amino benzoic acid were reacted on Au surfaces, with further post-functionalization by chemical reaction of the osmium complex amino-pyridine derivative with the surface carboxylates. The resulting modified Au surfaces were characterized by polarization modulated infrared reflection absorption spectroscopy (PM-IRRAS), scanning tunneling microscopy (STM), X-ray photoelectron spectroscopy (XPS), resonant raman spectroscopy and cyclic voltammetry.

Effects of the nature and charge of the topmost layer in layer by layer self assembled amperometric enzyme electrodes.

Organized layer-by-layer nanostructured amperometric enzyme electrodes with self-contained redox polyelectrolyte mediators have shown important effects depending on the nature and charge of the adsorbed topmost layer. Adsorption of PVS causes the drop of the catalytic responses to negligible values due to hindrance in electron hopping and enzyme wiring.

Wired-enzyme core-shell Au nanoparticle biosensor.

We report a fully integrated core-shell nanoparticle system responsive to glucose. The system is comprised of self-assembled glucose oxidase and an osmium molecular wire on core-shell Au nanoparticles. Characterization of the functional nanoparticles by spectroscopy, quartz crystal microbalance and electrochemical techniques has shown that the catalytically active shell has a structure as designed and all components are active in the self-assembled multilayer shell. Furthermore, amperometric reagentless detection of glucose and contactless photonic biosensing by the Os(II) resonant Raman signal have been demonstrated. The enzymatic reduction of FAD by glucose and further reduction of the Raman silent Os(III) by FADH 2 yields a characteristic enzyme-substrate calibration curve in the millimolar range. Furthermore, coupling of electronic resonant Raman of the osmium complex with the SERS amplification by Au NPs plasmon resonance has been demonstrated which leads to an extra enhancement of the biosensor signal. We present a proof of concept extending the work done with planar surfaces to core-shell NPs as an advance in the design of glucose-responsive chemistry detected by SERS-like methods.

Oxidation-reduction dynamics in layer-by-layer self-assembled redox polyelectrolyte multilayer modified electrodes.

The oxidation-reduction dynamics of layer-by-layer (LbL) self-assembled redox polyelectrolyte multilayer films on electrodes has been studied by cyclic voltammetry, chrono-amperometry, electrochemical quartz crystal microbalance (EQCM), ellipsometry, and Fourier transform reflection-absorption infrared spectroscopy (FT-IRRAS). Thin layer electrochemistry with fast electron transfer at the underlying metal-film interface and charge propagation by electron hopping between adjacent redox sites in the finite thin film has been observed. An almost ideal cyclic voltammetry for a fixed number of redox sites in the thin surface film suggests that the multilayer can be fully oxidized and reduced in the time scale of the experiment (RT/vF > or = 0.05 sec). The electron hopping diffusion coefficient 3 x 10(-10) cm2 s(-1) was obtained from the chronoamperometric current transient and the ellipsometric thickness. Both cyclic voltammetry and potential step yield a surface osmium bipyridyl redox concentration of gamma Os = 4 x 10(-10) mol x cm(-2) for (PAH-Os)5(PVS)4 film. Exchange of ions and solvent occur simultaneously to the charge injection as revealed by the EQCM mass change and the ellipsometric thickness change. From the end-to-end mass-to-charge linear relationship, the molar mass of the ionic and neutral species exchanged largely exceeds the molar mass of any ions or solvent which suggests an important flux of solvent during redox switching. An initial "break in" effect is observed for the first oxidation-reduction cycles when a newly self-assembled film equilibrates with the electrolyte as charge is injected during the electrochemical perturbation.

Characterization of self-assembled redox polymer and antibody molecules on thiolated gold electrodes.

Multilayer immobilization of antibody and redox polymer molecules on a gold electrode was achieved, as a strategy for the potential development of an amperometric immunosensor. The step-by-step assembly of antibiotin IgG on Os(bpy)(2)ClPyCH(2)NH poly(allylamine) redox polymer (PAH-Os) adsorbed on thiolated gold electrodes was proved by quartz crystal microbalance (QCM) and atomic force microscopy (AFM) experiments, confirming the electrochemical evidence. The increase of redox charge during the layer-by-layer deposition demonstrated that charge propagation within the layers is feasible. The multilayer structure proved to be effective for the molecular recognition of horseradish peroxidase-biotin conjugate (HRP-biotin), as confirmed by the QCM measurements and the electrocatalytic reduction current obtained upon H(2)O(2) addition. The catalytic current resulting from PAH-Os mediation was shown to increase with the number of assembled layers. Furthermore, the inventory of IgG molecules on the supramolecular self-assembled structure and the specific and non-specific binding of HRP-biotin conjugate were confirmed by the QCM transient studies, giving information on the kinetics of IgG deposition and HRP-biotin conjugate binding to the IgG.

Extracting kinetic parameters for homogeneous [Os(bpy)2ClPyCOOH]+ mediated enzyme reactions from cyclic voltammetry and simulations.

The homogeneous reaction between glucose oxidase and osmium bipyridine-pyridine carboxylic acid in the presence of glucose has been studied in detail by cyclic voltammetry and digital simulation. Combination of the analytical equations that describe the dependence of the amperometric response on enzyme, substrate and co-substrate concentrations for the limiting cases with digital simulation of the coupled enzyme reaction diffusion problem allows us to extract kinetic parameters for the substrate-enzyme reaction: K(MS)=10.8 mM, k(cat)=254 s(-1) and for the redox mediator-enzyme reaction, k=2.2x10(5) M(-1) s(-1). The accurate determination of the kinetic parameters at low substrate concentrations (<7 mM) is limited by depletion of the substrate close to the electrode surface. At high substrate concentrations (>20 mM) inactivation of the reduced form of glucose oxidase in the bulk solution must be taken into account in the analysis of the results.

Relaxation and Simplex mathematical algorithms applied to the study of steady-state electrochemical responses of immobilized enzyme biosensors: Comparison with experiments.

A description of the implementation of the relaxation method with automatic mesh point allocation for immobilized enzyme electrodes is presented. The advantages of this method for the solution of coupled reaction-diffusion problems are discussed. The relaxation numerical simulation technique is combined with the Simplex fitting algorithm to extract kinetic parameters from experimental data. The results of the simulations are compared to experimental data from self-assembled multilayered electrodes comprised of glucose oxidase (GOx) and an Os modified redox mediator and found to be in excellent agreement.

Electrochemical quartz crystal impedance study of redox hydrogel mediators for amperometric enzyme electrodes.

Quartz crystal impedance around the resonant frequency at 10 MHz of a composite quartz crystal resonator has been studied simultaneously with cyclic voltammetry. A modified quartz crystal with a redox hydrogel (poly(allylamine)-ferrocene cross-linked with glucose oxidase) and immersed in liquid electrolyte was used. Impedance parameters (R(f) and X(L)((f))) of the surface redox gel film were obtained by fitting the resonator transfer function |V(o)/V(i)| vs ω to a BVD equivalent circuit and analyzed with the multiple nonpiezoelectric layer model of Martin. Two limiting hydrogel layers of the same composition were studied while oxidizing and reducing the ferrocene/ferricenium moieties attached to the swollen polymer backbone: thin and thick redox hydrogel films. For the thin films, the Sauerbrey approximation was valid. The mass/thickness and film viscosity changes that resulted from the anion and water exchange were evaluated while redox switching the polymer on the assumption of negligible storage modulus G' and a density of 1. For thick gel layers, on the other hand, the penetration depth of the acoustic wave was far less than the film thickness, and a liquid-like behavior was apparent. Film storage modulus and film loss modulus were simultaneously evaluated with the cyclic voltammetry.

Electrochemical behavior of polyphenol oxidase immobilized in self-assembled structures layer by layer with cationic polyallylamine.

We report here a novel bioelectrode based on self-assembled multilayers of polyphenol oxidase intercalated with cationic polyallylamine built up on a thiol-modified gold surface. We use an immobilization strategy previously described by Hodak J. et al. (Langmuir 1997, 13, 2708-2716) Quartz crystal microbalance with electroacustic impedance experiments were carried out to follow quantitatively the multilayer film formation. The response of the self-assembly polyphenol oxidase-polyallylamine electrodes toward different metabolically related catecholamines was studied, to evaluate enzyme kinetics. For the analyzed compounds, only dopamine and its metabolite Dopac gave catalytic currents at applied potential close to 0 V. These responses were proportional to the number of polyphenol oxidase-immobilized layers and were also controlled by the enzymatic reaction. The combination of microgravimetric and electrochemical techniques allowed us to determine the kinetic enzymatic constants, showing that the decomposition rate for the enzyme-substrate complex is slower than the enzymatic reoxidation step.

Electrical Communication between Electrodes and Enzymes Mediated by Redox Hydrogels.

Different redox polymers based on poly(allylamine) with covalently attached ferrocene and pyridine groups that coordinate iron and ruthenium complexes were prepared, and hydrogels were obtained by cross-linking them with epichlorohydrin. Charge propagation from the underlying electrode, through the redox polymer and electrical communication with the enzyme FADH(2) of glucose oxidase, was studied by cyclic voltammetry and electrochemical impedance spectroscopy. The effects of electrolyte composition, concentration of enzyme and substrate, and electrode potential are reported. The role of different redox mediators covalently attached to the polymer backbone is discussed in terms of driving force and electrostatic barriers.

Effect of ionic strength on the behavior of amperometric enzyme electrodes mediated by redox hydrogels.

The electron-transfer behavior of electroactive hydrogels formed by cross-linking ferrocene poly(allylamine) (Fc-PAA) and glucose oxidase is investigated as a function of electrolyte ionic strength using several techniques. Cyclic voltammetry and electrochemical impedance spectroscopy show that the quantity cD(e)(1/2) increases with electrolyte concentration. Enhancement of enzyme catalysis for the oxidation of glucose mediated by Fc-PAA is also apparent at higher KNO(3) concentration. The electroactive redox center concentration, c, and the diffusion coefficient due to electron hopping in the gel, D(e), are independently measured by chronoamperometry at ultramicroelectrodes. Larger electrolyte ionic strength induces an increase in electroactive redox center concentration while D(e) slightly decreases. These results are rationalized in terms of the electrostatic interactions within the redox gel backbone due to water and ion exchange with the external electrolyte, producing swelling and shrinking of the hydrogel.

Layer-by-layer electrostatic deposition of biomolecules on surfaces for molecular recognition, redox mediation and signal generation.

Layer-by-layer supramolecular structures composed of alternate layers of negatively charged enzymes and cationic redox polyelectrolyte have been assembled. Glucose oxidase (GOx), lactate oxidase (LOx) and soybean peroxidase (SBP) have been electrically wired to the underlying electrode by means of poly(allylamine) with [Os(bpy)2ClPyCOH]+ covalently attached (PAA-Os) in organized structures with high spatial resolution. Biotinylated glucose oxidase has also been used to assemble step-by-step on antibiotin goat immunoglobulin (IgG) layers and the enzyme was electrically wired by PAA-Os. These spatially organized multilayers with mono- and bienzymatic schemes can work efficiently in molecular recognition, redox mediation and generation of an electrical signal. The concentration of redox mediator integrated into the multilayers, obtained from the voltammetric charge and an estimation of the layer thickness, exceeds by 100-fold the amount of deposited enzyme assessed by quartz crystal microbalance. Differences in GOx electrical wiring efficiency have been detected with the different assembling strategies. The surface concentration of electrically wired enzyme represents a small proportion of all the enzyme molecules present in the multilayers which can be oxidized by the soluble mediator [Os(bpy)2Cl PyCOOH]Cl. This proportion, as well as the rate of FADH2 oxidation by PAA-Os, increases with the number of electrically wired enzyme layers and with the spatial accessibility of the Os moiety to the enzyme active center.

Layer-by-layer self-assembly of glucose oxidase and Os(Bpy)2CIPyCH2NH-poly(allylamine) bioelectrode.

The uptake of glucose oxidase (GOx) onto a polycationic redox polymer (PAA-Os)-modified surface, by adsorption from dilute aqueous GOx solutions, was followed by the quartz crystal microbalance (QCM) and shows double exponential kinetics. The electrochemistry of the layer-by-layer-deposited redox-active polymer was followed by cyclic voltammetry in glucose-free solutions, and the enzyme catalysis mediated by the redox polymer was studied in beta-D-glucose-containing solutions. AFM studies of the different layers showed the existence of large two dimension enzyme aggregates on the osmium polymer for 1 microM GOx and less aggregation for 50 nM GOx solutions. When the short alkanethiol, 2,2'-diaminoethyldisulfide was preadsorbed onto gold, a monoexponential adsorption law was observed, and single GOx enzyme molecules could be seen on the surface where the enzyme was adsorbed from 50 nM GOx in water.