STM study of morphology and electron transport features in cytochrome c and nanocluster molecule monolayers.

The morphology and electron tunneling through single cytochrome c and nanocluster Pt(5)(CO)(7)[P(C(6)H(5))](4) molecules organized as monolayer Langmuir-Blodgett (LB) films on graphite substrate have been studied experimentally using scanning tunneling microscopy (STM) and spectroscopy techniques with sub-nanometer spatial resolution in a double barrier tunnel junction configuration STM tip-monomolecular film-conducting substrate at ambient conditions. STM images of the films revealed globular structures with characteristic diameters (approximately 3.5 nm for the protein molecule and approximately 1.2 nm for the nanocluster). The spectroscopic study by recording the tunneling current-bias voltage (I-V) curves revealed tunneling I-V characteristics with features as steps of different width and heights that are dependent on the STM tip position over the molecule in the monolayer, giving evidence for sequential discrete electron-tunneling effects with the combination of the single electron Coulomb-charging energy and the electronic energy level separation (molecular spectrum) in such immobilized metalloprotein and nanocluster structures that can be of interest for the development of bioelectronic and hybrid functional nanosystems.     

Intermolecular coupling in nanometric domains of light-harvesting dendrimer films studied by photoluminescence near-field scanning optical microscopy (PL NSOM)

Near-field scanning optical microscopy (NSOM) has been used to investigate the photophysical characteristics of first- to fourth-generation (G1 to G4) light-harvesting dendrimer thin films containing coumarin-343 and coumarin-2 as the core and peripheral chromophores, respectively. Thin film photoluminescence (PL) spectra exhibit a significant red shift in the lower generations (G1, G2, and G3) as compared to their respective solution PL spectra, implying the formation of excimers. Spatially resolved PL NSOM images exhibit pronounced nanoscopic domains in G1, which become more homogeneous in higher generations due to site-isolation of the core chromophore. G4 exhibits complete site-isolation for these light-harvesting dendrimer films.     

铁氰化钴/树状高分子修饰电极免标记法检测基因突变

利用铁氰化钴/树状高分子(CoHCF/PAMAM)复合材料修饰玻碳电极(GCE), 制备了免标记检测基因突变的新型DNA电化学传感器. 传感器中树状高分子层明显增加了单链DNA探针的固定量, 铁氰化钴层增大了鸟嘌呤的氧化信号, 该传感器可以灵敏识别单碱基错配的基因序列, 具有良好的选择性和灵敏度. 在7.6×10^-11～3.05×10^-8 mol/L浓度范围内, 鸟嘌呤(G)的氧化峰电流差值与突变基因浓度呈良好的线性关系, 检出限为1.0×10^-11 mol/L(S/N=3).     

A peptide dendrimer enzyme model with a single catalytic site at the core

Catalytic esterase peptide dendrimers with a core active site were discovered by functional screening of a 65,536-member combinatorial library of third-generation peptide dendrimers using fluorogenic 1-acyloxypyrene-3,6,8-trisulfonates as substrates. In the best catalyst, RMG3, ((AcTyrThr)(8)(DapTrpGly)(4)(DapArgSerGly)(2)DapHisSerNH2), ester hydrolysis is catalyzed by a single catalytic histidine residue at the dendrimer core. A pair of arginine residues in the first-generation branch assists substrate binding. The catalytic proficiency of dendrimer RMG3 (kcat/KM = 860 M(-1) min(-1) at pH 6.9) per catalytic site is comparable to that of the multivalent esterase dendrimer A3 ((AcHisSer)(8)(DapHisSer)(4)(DapHisSer)2DapHisSerNH2) which has fifteen histidines and five catalytic sites (Delort, E. et al. J. Am. Chem. Soc. 2004, 126, 15642-15643). Remarkably, catalysis in the single site dendrimer RMG3 is enhanced by the outer dendritic branches consisting of aromatic amino acids. These interactions take place in a relatively compact conformation similar to a molten globule protein as demonstrated by diffusion NMR. In another dendrimer, HG3 ((AcIlePro)(8)(DapIleThr)(4)(DapHisAla)(2)DapHisLeuNH2) by contrast, catalysis by a core of three histidine residues is unaffected by the outer dendritic layers. Dendrimer HG3 or its core HG1 exhibit comparable activity to the first-generation dendrimer A1 ((AcHisSer)(2)DapHisSerNH2). The compactness of dendrimer HG3 in solution is close to that a denatured peptide. These experiments document the first esterase peptide dendrimer enzyme models with a single catalytic site and suggest a possible relationship between packing and catalysis in these systems.     

Folding control and unfolding free energy of yeast iso-1-cytochrome c bound to layered zirconium phosphate materials monitored by surface plasmon resonance

The free energy change (Delta G degrees ) for the unfolding of immobilized yeast iso-1-cytochrome c (Cyt c) at nanoassemblies was measured by surface plasmon resonance (SPR) spectroscopy. Data show that SPR is sensitive to protein conformational changes, and protein solid interface exerts a major influence on bound protein stability. First, Cyt c was self-assembled on the Au film via the single thiol of Cys-102. Then, crystalline sheets of layered alpha-Zr(O(3)POH)(2).H(2)O (alpha-ZrP) or Zr(O(3)PCH(2)CH(2)COOH)(2).xH(2)O (alpha-ZrCEP) were adsorbed to construct alpha-ZrP/Cyt c/Au or alpha-ZrCEP/Cyt c/Au nanoassemblies. The construction of each layer was monitored by SPR, in real time, and the assemblies were further characterized by atomic force microscopy and electrochemical studies. Thermodynamic stability of the protein nanoassembly was assessed by urea-induced unfolding. Surprisingly, unfolding is reversible in all cases studied here. Stability of Cyt c in alpha-ZrP/Cyt c/Au increased by approximately 4.3 kJ/mol when compared to the unfolding free energy of Cyt c/Au assembly. In contrast, the protein stability decreased by approximately 1.5 kJ/mol for alpha-ZrCEP/Cyt c/Au layer. Thus, OH-decorated surfaces stabilized the protein whereas COOH-decorated surfaces destabilized it. These data quantitate the role of specific functional groups of the inorganic layers in controlling bound protein stability.     

Gene Delivery into T-Cells Using Ternary Complexes of DNA,Lipofectamine, and Carboxy-Terminal Phenylalanine-Modified Dendrimers

T-cells play critical roles in various immune reactions, and genetically engineered T-cells have attracted attention for the treatment of cancer and autoimmune diseases. Previously, it is shown that a polyamidoamine dendrimer of generation 4 (G4), modified with 1,2-cyclohexanedicarboxylic anhydride (CHex) and phenylalanine (Phe) (G4-CHex-Phe), is useful for delivery into T-cells and their subsets. In this study, an efficient non-viral gene delivery system is constructed using this dendrimer. Ternary complexes are prepared using different ratios of plasmid DNA, Lipofectamine, and G4-CHex-Phe. A carboxy-terminal dendrimer lacking Phe (G3.5) is used for comparison. These complexes are characterized using agarose gel electrophoresis, dynamic light scattering, and ζpotential measurements. In Jurkat cells, the ternary complex with G4-CHex-Phe at a P/COOH ratio of 1/5 shows higher transfection activity than other complexes, such as binary and ternary complexes with G3.5, without any significant cytotoxicity. The transfection efficiency of the G4-CHex-Phe ternary complexes decreases considerably in the presence of free G4-CHex-Phe and upon altering the complex preparation method. These results suggest that G4-CHex-Phe promotes the cellular internalization of the complexes, which is useful for gene delivery into T-cells.     

Thermal decomposition of generation-4 polyamidoamine dendrimer films: decomposition catalyzed by dendrimer-encapsulated Pt particles

The thermal decomposition of hydroxyl-terminated generation-4 polyamidoamine dendrimer (G4OH) films deposited on Au surfaces has been compared with decomposition of the same dendrimer encapsulating an approximately 40-atom Pt particle (Pt-G4OH). Infrared absorption reflection spectroscopy studies showed that, when the films were heated in air to various temperatures up to 275 degrees C, the disappearance of the amide vibrational modes occurred at lower temperature for the Pt-G4OH film. Dendrimer decomposition was also investigated by thermogravimetric analysis (TGA) in both air and argon atmospheres. For the G4OH dendrimer, complete decomposition was achieved in air at 500 degrees C, while decomposition of the Pt-G4OH dendrimer was completed at 400 degrees C, leaving only platinum metal behind. In a nonoxidizing argon atmosphere, a greater fraction of the G4OH decomposed below 300 degrees C, but all of the dendrimer fragments were not removed until heating above 550 degrees C. In contrast, Pt-G4OH decomposition in argon was similar to that in air, except that decomposition occurred at temperatures approximately 15 degrees C higher. Thermal decomposition of the dendrimer films on Au surfaces was also studied by temperature programmed desorption (TPD) and X-ray photoelectron spectroscopy (XPS) under ultrahigh vacuum conditions. Heating the G4OH films to 250 degrees C during the TPD experiment induced the desorption of large dendrimer fragments at 55, 72, 84, 97, 127, 146, and 261 amu. For the Pt-G4OH films, mass fragments above 98 amu were not observed at any temperature, but much greater intensities for H(2) desorption were detected compared to that of the G4OH film. XPS studies of the G4OH films demonstrated that significant bond breaking in the dendrimer did not occur until temperatures above 250 degrees C and heating to 450 degrees C caused dissociation of C=O, C-O, and C-N bonds. For the Pt-G4OH dendrimer films, carbon-oxygen and carbon-nitrogen bond scission was observed at room temperature, and further decomposition to atomic species occurred after heating to 450 degrees C. All of these results are consistent with the fact that the Pt particles inside the G4OH dendrimer catalyze thermal decomposition, allowing dendrimer decomposition to occur at lower temperatures. However, the Pt particles also catalyze bond scission within the dendrimer fragments so that decomposition of the dendrimer to gaseous hydrogen is the dominant reaction pathway compared to desorption of the larger dendrimer fragments observed in the absence of Pt particles.     

Preparation, characterization, resistance to protein adsorption, and specific avidin-biotin binding of poly(amidoamine) dendrimers functionalized with oligo(ethylene glycol) on gold

Protein-resistant films derived from the fifth-generation poly(amidoamine) dendrimers (PAMAM G5) functionalized with oligo(ethylene glycol) (OEG) derivatives consisting of various ethylene glycol units (EG(n), n = 3, 4, and 6) were prepared on the self-assembled monolayers (SAMs) of 11-mercaptoundecanoic acid (MUA) on gold substrates. The resulting films were characterized by ellipsometry, contact angle goniometry, and X-ray photoelectron spectroscopy (XPS). About 35% of the peripheral amines of the dendrimers were reacted with N-hydroxysuccinimide-terminated EG(n) derivatives (NHS-EG(n)). The dendrimer films showed improved stability over octadecanethiolate SAMs on gold in hot solvents, attributed to the formation of multiple amide bonds per PAMAM unit with underlying NHS-activated MUA monolayer. The EG(n)-attached PAMAM surfaces with n = 3 reduced the adsorption of fibrinogen to approximately 20% monolayer, whereas 2-3% for n = 4 or 6. The dendrimer films with various densities of EG(n) molecules on PAMAM surfaces were prepared by immersion of the NHS-terminated MUA-functionalized gold substrates in ethanolic solutions containing PAMAM and NHS-EG(n) of various mole ratios. The density (r) of the EG(n) molecules on the PAMAM surfaces is consistent with the mole ratio (r') of NHS-EG(n)/free amine of PAMAM in solutions. The resistance to protein adsorption of the resulting surfaces is correlated with the surface density and the length of the EG chains. At their respective r, the EG(n)-modified dendrimer films resisted approximately 95% adsorption of fibrinogen on gold surfaces. Finally, the specific binding of avidin to the approximately 5% and approximately 40% biotinylated EG3 dendrimers (surface density of biotin with respect to the total number of terminal amino groups on PAMAM G5) gave rise to about 50% and 100% surface coverage by avidin, respectively.     

Cobaltocenium-functionalized poly(propylene imine) dendrimers: redox and electromicrogravimetric studies and AFM imaging

The first four generations of cobaltocenium-functionalized, diaminobutane-based poly(propylene imine) dendrimers DAB-dend-Cb,(PFb)x (x = 4, 8, 16, and 32; Cb=[Co(eta5-C5H4CONH)(eta5-C5H5)] (1-4) have been synthesized and characterized. The redox activity of the cobaltocenium centers in 1-4 has been characterized by using cyclic voltammetry and the electrochemical quartz-crystal microbalance (EQCM). All of the dendrimers exhibit reversible redox chemistry associated with the cobaltocenium/cobaltocene redox couple. Upon reduction. the dendrimers exhibit a tendency to electrodeposit onto the electrode surface, which is more pronounced for the higher generations. Pt and glassy carbon electrodes could be modified with films derived from 1-4,exhibiting a well-defined and persistent electrochemical response. EQCM measurements show that the dendrimers adsorb, at open circuit, onto platinum surfaces at monolayer or submonolayer coverage. Cathodic potential scanning past -0.75 V at which the cobaltocenium sites are reduced, gave rise to the electrodeposition of multilayer equivalents of the dendrimers. The additional material gradually desorbs upon re-oxidation so that only a monolayer equivalent remains on the electrode surface. Changes in film morphology as a function of dendrimer generation and surface coverage were studied by using admittance measurements of the quartz-crystal resonator on the basis of its electrical equivalent circuit, especially in terms of its resistance parameter. In general, we find that films of the lower dendrimer generation 1 behave rigidly, whereas those of the higher generation 4 exhibit viscoelastic behavior with an intermediate behavior being exhibited by 2 and 3. Using tapping-mode atomic force microscopy (AFM). we have been able to obtain molecularly resolved images of dendrimer 4 adsorbed on a Pt(111) electrode.     

From model compounds to protein binding: syntheses, characterizations and fluorescence studies of [RuII(bipy)(terpy)L]2+ complexes (bipy = 2,2'-bipyridine; terpy = 2,2':6',2''-terpyridine; L = imidazole, pyrazole and derivatives, cytochrome c)

Compounds [RuII(bipy)(terpy)L](PF6)2 with bipy = 2,2'-bipyridine, terpy = 2,2':6',2"-terpyridine, L = H2O, imidazole (imi), 4-methylimidazole, 2-methylimidazole, benzimidazole, 4,5-diphenylimidazole, indazole, pyrazole, 3-methylpyrazole have been synthesized and characterized by 1H NMR, ESI-MS and UV/Vis (in CH3CN and H2O). For L = H2O, imidazole, 4,5-diphenylimidazole and indazole the X-ray structures of the complexes have been determined with the crystal packing featuring only few intermolecular C-H...pi or pi-pi interactions due to the separating action of the PF6-anions. Complexes with L = imidazole and 4-methylimidazole exhibit a fluorescence emission with a maximum at 662 and 667 nm, respectively (lambdaexc= 475 nm, solvent CH3CN or H2O). The substitution of the aqua ligand in [Ru(bipy)(terpy)(H2O)]2+ in aqueous solution by imidazole to give [Ru(bipy)(terpy)(imi)]2+ is fastest at a pH of 8.5 (as followed by the increase in emission intensity). Coupling of the [Ru(bipy)(terpy)]2+ fragment to cytochrome c(Yeast iso-1) starting from the Ru-aqua complex was successful at 35 degrees C and pH 7.0 after 5 d under argon in the dark. The [Ru(bipy)(terpy)(cyt c)]-product was characterized by UV/Vis, emission and mass spectrometry. The location where the [Ru(bipy)(terpy)] complex was coupled to the protein was identified as His44 (corresponding to His39 in other numbering schemes) using digestion of the Ru-coupled protein by trypsin and analysis of the tryptic peptides by HPLC-high resolution MS.     

Immobilization of cytochrome c on cysteamine-modified gold electrodes with EDC as coupling agent

Cyclic voltammetry has been applied for the characterization of cross-linked horse heart cytochrome c (HHC) on cysteamine-modified gold electrodes. The cross-linking, i.e. amide bond formation, between the proteins was achieved by using 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) as coupling reagent. The optimal conditions for the formation of the HHC film were determined by varying the HHC concentration. In addition the reproducibility, stability and the influence of the scan rate upon these films were investigated with cyclic voltammetry. The protein film stability in a 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) buffer solution was tested by UV/vis absorption spectroscopy.     

Properties of mixed alkanethiol-dendrimer layers and their applications in biosensing

We studied the properties of mixed alkanethiol-dendrimer layers on a gold support and their application in biosensing. We showed that properties of glucose sensor can be modified using a different ratio of 1-hexadecanethiol (HDT) and poly(amidoamine) dendrimer of first generation (G1). The cyclic voltammetry in the presence of the redox couple, Fe(CN)(6)(3-)/Fe(CN)(6)(4-), was used for estimating how effectively the layer blocks the redox probe's access to the electrode surface. A scanning electrochemical microscope (SECM) was used to image the resulting distribution of the organic compounds. We found that with increasing content of dendrimers, the integrity of the layers was improved.     

Bienzyme sensors based on novel polymethylferrocenyl dendrimers

Amperometric bienzyme electrodes with horseradish peroxidase (HRP) and glucose oxidase (GOx) co-immobilized on polymethylferrocenyl dendrimers deposited onto platinum electrodes have been used for determination of the hydrogen peroxide produced by the oxidase during the enzymatic reaction. The redox dendrimers consist of flexible poly(propylenimine) dendrimer cores functionalised with octamethylferrocenyl units. The effects of dendrimer generation, the thickness of the dendrimer layer, substrate concentration, interferences, and reproducibility on the response of the sensors were investigated. The new bienzyme biosensors respond to substrate at work potential values between 200 and 50 mV (vs. SCE), have good sensitivity, and are resistant to interferences. Figure     

Efficient direct electron transfer with enzyme on a nanostructured carbon film fabricated with a maskless top-down UV/ozone process

We have developed a new carbon film electrode material with thornlike surface nanostructures to realize efficient direct electron transfer (DET) with enzymes, which is very important for various enzyme biosensors and for anodes or cathodes used in biofuel cells. The nanostructures were fabricated using UV/ozone treatment without a mask, and the obtained nanostructures were typically 2-3.5 nm high as confirmed by atomic force microscopy measurements. X-ray photoelectron spectroscopy and transmission electron microscopy revealed that these nanostructures could be formed by employing significantly different etching rates depending on nanometer-order differences in the local sp(3) content of the nanocarbon film, which we fabricated with the electron cyclotron resonance sputtering method. These structures could not be realized using other carbon films such as boron-doped diamond, glassy carbon, pyrolyzed polymers based on spin-coated polyimide or vacuum-deposited phthalocyanine films, or diamond-like carbon films because those carbon films have relatively homogeneous structures or micrometer-order crystalline structures. With physically adsorbed bilirubin oxidase on the nanostructured carbon surface, the DET catalytic current amplification was 30 times greater than that obtained with the original carbon film with a flat surface. This efficient DET of an enzyme could not be achieved by changing the hydrophilicity of the flat carbon surface, suggesting that DET was accelerated by the formation of nanostructures with a hydrophilic surface. Efficient DET was also observed using cytochrome c.     

Preparation and characterization of polyoxometalate/protein ultrathin films grown on electrode surfaces using layer-by-layer assembly

We report a new electrostatic layer-by-layer assembly method for the controlled deposition of electrocatalytically active enzymes onto electrode surfaces using polyoxometalate as the counteranion. Cytochrome c (cyt c), a redox active protein, and P(2)W(18)O(62)(6-), a Dawson-type polyoxometalate, were deposited onto glassy carbon electrodes by two procedures: static dipping and electrochemical cycling. Cyclic voltammetry and UV-vis spectroscopy reveal that approximately 1.5 x 10(-10) mol/cm(2) of P(2)W(18)O(62)(6-) and 2.2 x 10(-11) mol/cm(2) of cytochrome c are deposited per cycle, which correspond to approximately one monolayer of each molecule. The thicknesses of the resulting films measured by atomic force microscopy also indicate that the films are formed in a layer-by-layer fashion. Experimental factors that affect electron-transfer rate in these films, such as scan rate and film thickness, were systematically analyzed. The use of {P(2)W(18)O(62)(6-)/cyt c}n films to catalyze hydrogen peroxide reduction was demonstrated.     

Charge mediation by ruthenium poly(pyridine) complexes in 'second-generation' glucose biosensors based on carboxymethylated β-cyclodextrin polymer membranes

Four different poly(pyridine) complexes of ruthenium, viz. Ru(II)(trpy)(phen)(OH(2))](2+) (1), trans-[Ru(III)(2,2'bpy)(2)(OH(2))(OH)](2+) (2), [(2,2'bpy)(2)(OH)Ru(III)ORu(III)(OH)(2,2'bpy)(2)](4+) (3), and [Ru(II)(4,4'bpy)(NH(3))(5)](2+) (4) (2,2'bpy=2,2'-bipyridine, 4,4'bpy=4,4'-bipyridine, trpy=2,2',2"-terpyridine, phen=1,10-phenanthroline), were tested as non-physiological charge mediators of 'second-generation' glucose biosensors. The membranes for these biosensors were prepared by casting anionic carboxymethylated beta-cyclodextrin polymer films (beta-CDPA) directly onto the Pt or glassy carbon (GC) disk electrodes. Simultaneously, glucose oxidase (GOD) was immobilized in the films by covalent bonding and the Ru complexes were incorporated both by inclusion in the beta-CD molecular cavities and by ion exchange at the fixed carboxymethyl cation-exchange sites. The leakage of the mediator from the polymer has been minimized by adopting a suitable pre-treatment procedure. The biosensors catalytic activities increased in the order 1<2<3<4, as established by linear sweep voltammetry. In case of complexes 2-4, the enzymatic glucose oxidation was mediated by the Ru complexes at their redox potentials. However, this oxidation was mediated by oxygen in case of complex 1 where H(2)O(2) was detected as the reaction product. The effectiveness of the mediators used in the presence of oxygen has been estimated using Pt and GC supports. The redox potential of the mediator does not depend on the support used, while the oxidation of H(2)O(2) proceeds on GC at much higher positive potentials than on Pt. The sensitivity and the linear concentration range of the biosensor studied varied significantly. For complex 4, which forms stable inclusion complex with beta-CD, the biosensor sensitivity was the highest and equal to 7.2 micro A mM(-1) cm(-2), detectability was as low as 1 mM, but the linear concentration range was limited only to 4 mM. In contrast, for complexes 2 and 3 the sensitivity was 0.4 and 3.2 micro A mM(-1) cm(-2), while the linear concentration range extended up to at least 24 and 14 mM glucose, respectively. Even though some common interfering substances, such as ascorbate, paracetamol or urea, are oxidized at potentials close to those of the Ru complex redox couples, their electro-oxidation currents at physiological concentrations are insignificant compared to those due to the biocatalytic oxidation of glucose. The biosensor response to glucose is reversible as demonstrated by the inhibition of GOD activity by Cu(II). That is, the Cu(II) concentration required to inhibit by half the response to glucose of the biosensor containing complex 2 was 1.0 mM. This inhibitory effect was fully reversed by addition of citrate, a ligand forming sufficiently stable complex with Cu(II).     

Direct electrochemistry of cytochrome c immobilized on a novel macroporous gold film coated with a self-assembled 11-mercaptoundecanoic acid monolayer

We have successfully constructed a novel gold film with open interconnected macroporous walls of nanoparticles by combining the hydrogen bubble dynamic template synthesis with galvanic replacement reaction. After modified by a self-assembled monolayer (SAM) of 11-mercaptoundecanoic acid (MUA), the three-dimensionally (3D) interconnected macroporous Au film has been used as a biocompatible substrate for the immobilization of cytochrome c. The morphology, structure and electrochemical features of the modified and unmodified macroporous Au films were characterized by field-emission scanning electron microscopy (FESEM), energy-dispersive X-ray (EDX), cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). The results reveal that the resultant films had a large electroactive surface area for high protein loading, enhanced electron transfer of cytochrome c, retained electrochemical activity, good stability and repeatability. And the excellent electrochemical behaviors could be attributed to the hierarchical structure of the macroporous Au film constructed by nanoparticles.     

Investigation of novel mediators for a glucose biosensor based on metal picolinate complexes

The metal complexes [Os(byp)(2)(pic)](+) and [Ru(byp)(2)(pic)](+) where byp is 2,2'-bipyridine and HPic is o-picolinic acid were synthesised and characterised using spectroscopic and electrochemical techniques. These complexes were then evaluated as mediators for a glucose oxidase (GOx)-based biosensor. Results demonstrate the electrocatalytic behaviour of both metal couples towards regeneration of the flavoprotein GOx (FADH(2)) group, when co-immobilised with glucose oxidase. Surface immobilisation was achieved by potential cycling in aqueous solutions of the metal complexes at a glucose oxidase (GOx)/Nafion modified electrode. This proved successful in terms of catalytic efficiency and stability of redox sites. Kinetic parameters associated with both enzymatic and mediator reactions were estimated and the stability/performance properties of the sensor were tested.     

Synthesis and Characterization of Polyether Adducts of Barium and Strontium Carboxylates and Their Use in the Formation of MTiO(3) Films

The synthesis, characterization, and reactivity of new polyether adducts of strontium and barium carboxylates of general composition M(O(2)CCF(3))(n)()(L) (M = Ba, L = 15-crown-5, (1); M = Ba (2), Sr (3), respectively, with L = tetraglyme are reported. The compounds were synthesized by reaction of BaCO(3) or MH(2) (M = Sr or Ba) with organic acids in the presence of the polyether ligands. These compounds have been characterized by IR and (13)C and (1)H NMR spectroscopies, elemental analyses, and thermogravimetric analysis. The species Ba(2)(O(2)CCF(3))(4)(15-crown-5)(2) (1) and [Ba(2)(O(2)CCF(3))(4)(tetraglyme)](infinity) (2), were also characterized by single-crystal X-ray diffraction. Ba(2)(O(2)CCF(3))(4)(15-crown-5)(2) (1) crystallizes in the orthorhombic space group Cccm with cell dimensions of a = 13.949(1) ?, b = 19.376(2) ?, c = 16.029(1) ?, and Z = 8. [Ba(2)(O(2)CCF(3))(4)(tetraglyme)](infinity) (2) crystallizes in the monoclinic space group C2/c with cell dimensions of a = 12.8673(12) ?, b = 16.6981(13) ?, c = 15.1191(12) ?, beta = 99.049(8) degrees, and Z = 4. Compounds 1-3 thermally decompose at high temperatures in the solid state to give MF(2). However, solutions of compounds 1-3 dissolved in ethanol with Ti(O-i-Pr)(4) give crystalline perovskite phase MTiO(3) films, or in the case of mixtures of 2 and 3, Ba(1)(-)(x)()Sr(x)()TiO(3) films below 600 degrees C when spin coated onto silicon substrates and thermally treated. The crystallinity, purity, and elemental composition of the films was determined by glancing angle X-ray diffraction and Auger electron spectroscopy.     

Magnetic field effects on bioelectrocatalytic reactions of surface-confined enzyme systems: enhanced performance of biofuel cells

The effect of a constant magnetic field on bioelectrocatalytic transformations of three different enzyme assemblies linked to electrodes is examined and correlated with a theoretical magnetohydrodynamic model. The systems consist of surface-reconstituted glucose oxidase (GOx), an integrated lactate dehydrogenase/nicotinamide/pyrroloquinoline quinone assembly (LDH/NAD+ -PQQ), and a cytochrome c/cytochrome oxidase system (Cyt c/COx) linked to the electrodes. Pronounced effects of a constant magnetic field applied parallel to the electrode surface are observed for the bioelectrocatalyzed oxidation of glucose and lactate by the GOx-electrode and LDH/NAD+ -PQQ-electrode, respectively. The enhancement of the bioelectrocatalytic processes correlates nicely with the magnetohydrodynamic model, and the limiting current densities (iL) relate to B1/3 (B = magnetic flux density) and to C4/3 (C* = bulk concentration of the substrate). A small magnetic field effect is observed for the Cyt c/COx-electrode, and its origin is still questionable. The effect of the constant magnetic field on the performance of biofuel cells with different configurations is examined. For the biofuel cell consisting of LDH/NAD+ -PQQ anode and Cyt c/COx cathode, a 3-fold increase in the power output was observed at an applied magnetic field of B = 0.92 T and external load of 1.2 kOhms.