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Eugenii Katz

Publications and source records attributed to Eugenii Katz.

At least 19 recordsLinked to original sources
PubMed2004

Magnetic field effects on cytochrome c-mediated bioelectrocatalytic transformations.

Constant magnetic fields affect many biological transformations, but we lack mechanistic understanding of the processes. The magnetohydrodynamic effect may account for the enhancement of bioelectrocatalytic transformations at interfaces. This is exemplified by the bioelectrocatalyzed cytochrome c-mediated reduction of oxygen and oxidation of lactate in the presence of cytochrome oxidase and lactate dehydrogenase, respectively. We observe significant magnetic field effects on the rates of bioelectrochemical transformations (ca. 3-fold increase) at the functionalized interfaces at field strengths, B, up to 1 T. We show that the limiting current is proportional to the B(1/3)C*(4/3), where C is the concentration of electroactive species. The results may have important implications on the understanding of the magnetic field effects on natural biocatalytic processes at membranes and on the enhancement of biotransformations in biotechnology.

Animals↗
PubMed2004

Amplified telomerase analysis by using rotating magnetic particles: the rapid and sensitive detection of cancer cells.

A highly sensitive telomerase detection method that involves amplified telomerase analysis and the use of rotating magnetic particles has been developed. Magnetic particles, functionalized with a primer (1) that is recognized by telomerase, are mixed with a nucleotide mixture that includes biotinylated-dUTP, and telomerase-induced elongation of the primers proceeds with simultaneous biotin incorporation. Avidin-Horseradish peroxidase conjugate, coupled to biotin labels, yields the biocatalytic functional particles. Mixing the resulting particles with naphthoquinone-modified magnetic particles enables the optoelectronic detection of telomerase. Attraction of the magnetic particles to an electrode, followed by rotation of the particles, causes the electrocatalytic reduction of O(2) to H(2)O(2) and HRP-catalyzed oxidation of luminol (3); this results in chemilumunescence. The intensity of the emitted light depends on the telomerase content of the sample and the rotation speed of the particles. A minimum number of 10 cancer cells could be detected.

Adenocarcinoma↗
PubMed2004

Enzyme-catalyzed bio-pumping of electrons into au-nanoparticles: a surface plasmon resonance and electrochemical study.

The enzyme glucose oxidase (GOx) is reconstituted on a flavin adenin dinucleotide (FAD, 1) cofactor-functionalized Au-nanoparticle (Au-NP), 1.4 nm, and the GOx/Au-NP hybrid is linked to a bulk Au-electrode by a short dithiol, 1,4-benzenedithiol (2), or a long dithiol, 1,9-nonanedithiol (3), monolayer. The reconstituted GOx/Au-NP hybrid system exhibits electrical communication between the enzyme redox cofactor and the Au-NP core. Because the thiol monolayers provide a barrier for electron tunneling, the electron transfer occurring upon the biocatalytic oxidation of glucose results in the Au-NPs charging. The charging of the Au-NPs alters the plasma frequency and the dielectric constant of the Au-NPs, thus leading to the changes of the dielectric constant of the interface. These are reflected in pronounced shifts of the plasmon angle, theta(P), in the surface plasmon resonance (SPR) spectra. As the biocatalytic charging phenomenon is controlled by the concentration of glucose, the changes in the theta(P) values correlate with the concentration of glucose. The biocatalytic charging process is characterized by following the differential capacitance of the GOx/Au-NP interface and by monitoring the potential generated on the bulk Au-electrode. The charging of the GOx/Au-NPs is also accomplished in the absence of glucose by the application of an external potential on the electrode, that resulted in similar plasmon angle shifts. The results allowed us to estimate the number of electrons stored per Au-NP at variable concentrations of glucose in the presence of the two different thiol linkers.

Aspergillus niger↗
PubMed2003

Probing photoelectrochemical processes in Au-CdS nanoparticle arrays by surface plasmon resonance: application for the detection of acetylcholine esterase inhibitors.

The photoelectrochemical charging of Au-nanoparticles (NP) in a Au-nanoparticle/CdS-nanoparticle array assembled on a Au-coated glass surface is followed by means of surface plasmon resonance (SPR) spectroscopy upon continuous irradiation of the sample. The charging of the Au-NPs results in the enhanced coupling between the localized surface plasmon of the Au-NP and the surface plasmon of the bulk surface, leading to a shift in the plasmon angle. The charging effect of the Au-NPs is supported by concomitant electrochemical experiments in the dark. Analysis of the results indicates that ca. 4.2 electrons are associated with each Au-nanoparticle under steady-state irradiation. The photoelectrochemical charging effect of the Au-NPs in the Au-CdS NP array is employed to develop a SPR sensor for acetylcholine esterase inhibitors.

Animals↗
PubMed2003

Au nanoparticle-enhanced surface plasmon resonance sensing of biocatalytic transformations.

N-(3-Aminopropyl)-N'-methyl-4,4'-bipyridinium is coupled to tiopronin-capped Au nanoparticles (diameter ca. 2 nm) to yield methyl(aminopropyl)viologen-functionalized Au nanoparticles (MPAV(2+)-Au nanoparticles). In situ electrochemical surface plasmon resonance (SPR) measurements are used to follow the electrochemical deposition of the bipyridinium radical cation modified Au nanoparticles on an Au-coated glass surface and the reoxidation and dissolution of the bipyridinium radical cation film. The MPAV(2+)-functionalized Au nanoparticles are also employed for the amplified SPR detection of NAD(+) and NADH cofactors. By SPR monitoring the partial biocatalyzed dissolution of the bipyridinium radical cation film in the presence of diaphorase (DP) NAD(+) is detected in the concentration range of 1x10(-4) M to 2x10(-3) M. Similarly, the diaphorase-mediated formation of the bipyridinium radical cation film on the Au-coated glass surface by the reduction of the MPAV(2+)-functionalized Au nanoparticles by NADH is used for the amplified SPR detection of NADH in the concentration range of 1x10(-4) M to 1x10(-3) M.

Biotransformation↗
PubMed2003

Magnetic control of electrocatalytic and bioelectrocatalytic processes.

Bioelectronics is a rapidly progressing interdisciplinary research field that has important implications for the development of biosensors, biofuel cells, biomaterial-based computers, and bioelectronic devices. Magneto-controlled molecular electronics and bioelectronics are new topics that examine the effect of an external magnetic field on electrocatalytic and bioelectrocatalytic processes of functionalized magnetic particles associated with electrodes. In this article we describe the progress in the developments of magneto-switchable electrocatalytic and bioelectrocatalytic transformations, and the effects of the rotation of the magnetic particles on the electrocatalytic and bioelectrocatalytic processes are discussed. Finally, the implications of the results on the development of biosensors, amplified immunosensors, and DNA sensors are described.

Biosensing Techniques↗
PubMed2003

A biofuel cell with electrochemically switchable and tunable power output.

An electroswitchable and tunable biofuel cell based on the biocatalyzed oxidation of glucose is described. The anode consists of a Cu(2+)-poly(acrylic acid) film on which the redox-relay pyrroloquinoline quinone (PQQ) and the flavin adenine dinucleotide (FAD) cofactor are covalently linked. Apo-glucose oxidase is reconstituted on the FAD sites to yield the glucose oxidase (GOx)-functionalized electrode. The cathode consists of a Cu(2+)-poly(acrylic acid) film that provides the functional interface for the covalent linkage of cytochrome c (Cyt c) that is further linked to cytochrome oxidase (COx). Electrochemical reduction of the Cu(2+)-poly(acrylic acid) films (applied potential -0.5 V vs SCE) associated with the anode and cathode yields the conductive Cu(0)-poly(acrylic acid) matrixes that electrically contact the GOx-electrode and the COx/Cyt c-electrode, respectively. The short-circuit current and open-circuit voltage of the biofuel cell correspond to 105 microA (current density ca. 550 microA cm(-2)) and 120 mV, respectively, and the maximum extracted power from the cell is 4.3 microW at an external loading resistance of 1 kOmega. The electrochemical oxidation of the polymer films associated with the electrodes (applied potential 0.5 V) yields the nonconductive Cu(2+)-poly(acrylic acid) films that completely block the biofuel cell operation. By the cyclic electrochemical reduction and oxidation of the polymer films associated with the anode and cathode between the Cu(0)-poly(acrylic acid) and Cu(2+)-poly(acrylic acid) states, the biofuel cell performance is reversibly switched between "ON" and "OFF" states, respectively. The electrochemical reduction of the Cu(2+)-polymer film to the Cu(0)-polymer film is a slow process (ca. 1000 s) because the formation and aggregation of the Cu(0)-clusters requires the migration of Cu(2+) ions in the polymer film and their reduction at conductive sites. The slow reduction of the Cu(2+)-polymer films allows for the controlling of the content of conductive domains in the films and the tuning of the output power of the biofuel cell. The electron-transfer resistances of the cathodic and anodic processes were characterized by impedance spectroscopy. Also, the overall resistances of the biofuel cell generated by the time-dependent electrochemical reduction process were followed by impedance spectroscopy and correlated with the internal resistances of the cell upon its operation.

Bioelectric Energy Sources↗
PubMed2003

"Plugging into Enzymes": nanowiring of redox enzymes by a gold nanoparticle.

The reconstitution of an apo-flavoenzyme, apo-glucose oxidase, on a 1.4-nanometer gold nanocrystal functionalized with the cofactor flavin adenine dinucleotide and integrated into a conductive film yields a bioelectrocatalytic system with exceptional electrical contact with the electrode support. The electron transfer turnover rate of the reconstituted bioelectrocatalyst is approximately 5000 per second, compared with the rate at which molecular oxygen, the natural cosubstrate of the enzyme, accepts electrons (approximately 700 per second). The gold nanoparticle acts as an electron relay or "electrical nanoplug" for the alignment of the enzyme on the conductive support and for the electrical wiring of its redox-active center.

Apoenzymes↗
PubMed2003

Analysis of NAD(P)+/NAD(P)H cofactors by imprinted polymer membranes associated with ion-sensitive field-effect transistor devices and Au-quartz crystals.

Specific recognition sites for the NAD(P)+ and NAD(P)H cofactors are imprinted in a cross-linked acrylamide-acrylamidophenylboronic acid copolymer membrane. The imprinted membranes, associated with pH-sensitive field-effect transistors (ISFETs) or Au-quartz piezoelectric crystals, enable the potentiometric or microgravimetric analysis of the oxidized NAD(P)+ cofactors and the reduced NAD(P)H cofactors, respectively. The NAD+- and NADP+-imprinted membranes associated with the ISFET allow the analysis of NAD+ and NADP+ with sensitivities that correspond to 15.0 and 18.0 mVdecade(-1) and detection limits of 4 x 10(-7) and 2 x 10(-7) M, respectively. The NADH- and NADPH-imprinted membranes associated with the ISFET device enable the analysis of NADH and NADPH with sensitivities that correspond to 24.2 and 21.8 mV x decade(-1) and lower detection limits that are 1 x 10(-7) and 2 x 10(-7) M, respectively. The ISFET devices functionalized with the NADH and NADPH membranes are employed in the analysis of the biocatalyzed oxidation of lactic acid and ethanol in the presence of lactate dehydrogenase and alcohol dehydrogenase, respectively.

Binding Sites↗
PubMed2002

Electrical contacting of flavoenzymes and NAD(P)+-dependent enzymes by reconstitution and affinity interactions on phenylboronic acid monolayers associated with Au-electrodes.

The preparation of integrated, electrically contacted, flavoenzyme and NAD(P)(+)-dependent enzyme-electrodes is described. The reconstitution of apo-glucose oxidase, apo-GOx, on a FAD cofactor linked to a pyrroloquinoline quinone (PQQ) phenylboronic acid monolayer yields an electrically contacted enzyme monolayer (surface coverage 2.1 x 10(-)(12) mol cm(-)(2)) exhibiting a turnover rate of 700 s(-)(1) (at 22 +/- 2 degrees C). The system is characterized by microgravimetric quartz-crystal microbalance analyses, Faradaic impedance spectroscopy, rotating disk electrode experiments, and cyclic voltammetry. The performance of the enzyme-electrode for glucose sensing is described. Similarly, the electrically contacted enzyme-electrodes of NAD(P)(+)-dependent enzymes malate dehydrogenase, MalD, and lactate dehydrogenase, LDH, are prepared by the cross-linking of affinity complexes generated between the enzymes and the NADP(+) and NAD(+) cofactors linked to a pyrroloquinoline quinone phenylboronic acid monolayer, respectively. The MalD enzyme-electrode (surface coverage 1.2 x 10(-)(12) mol cm(-)(2)) exhibits a turnover rate of 190 s(-)(1), whereas the LDH enzyme-electrode (surface coverage 7.0 x 10(-)(12) mol cm(-)(2)) reveals a turnover rate of 2.5 s(-)(1). Chronoamperometric experiments reveal that the NAD(+) cofactor is linked to the PQQ-phenylboronic acid by two different binding modes. The integration of the LDH with the two NAD(+) cofactor configurations yields enzyme assemblies differing by 1 order of magnitude in their bioelectrocatalytic activities.

Animals↗
PubMed2002

Magneto-switchable electrocatalytic and bioelectrocatalytic transformations.

Magnetic switching of redox reactions and bioelectrocatalytic transformations is accomplished in the presence of relay-functionalized magnetite particles (Fe(3)O(4)). The electrochemistry of a naphthoquinone (1), pyrroloquinoline quinone (2; PQQ), microperoxidase-11 (3), a ferrocene derivative (4) and a bipyridinium derivative (5), functionalized magnetic particles, is switched "ON" and "OFF" by an external magnet upon the attraction of the magnetic particles to an electrode or their retraction from the electrode, respectively. The magneto-switchable activation and deactivation of the electrochemical oxidation of the ferrocene-functionalized magnetic particles and the electrochemical reduction of the bipyridinium-functionalized magnetic particles are used for the triggering of mediated bioelectrocatalytic oxidation of glucose, in the presence of glucose oxidase (GOx), and bioelectrocatalytic reduction of nitrate (NO(3) (-)), in the presence of nitrate reductase (NR), respectively. Magnetic particles functionalized with a PQQ-NAD(+) dyad are used for the magnetic switching of the bioelectrocatalytic oxidation of lactate in the presence of lactate dehydrogenase (LDH). The coupling of these particles with a ferrocene-monolayer-functionalized electrode allows the dual and selective sensing of lactate and glucose in the presence of LDH and GOx, respectively, by using an external magnet to switch the detection mode.

Journal Article↗
PubMed2002

Electrical contacting of glucose dehydrogenase by the reconstitution of a pyrroloquinoline quinone-functionalized polyaniline film associated with an Au-electrode: an in situ electrochemical SPR study.

A novel method to generate an integrated electrically contacted glucose dehydrogenase electrode by the surface reconstitution of the apo-enzyme on a pyrroloquinoline quinone (PQQ)-modified polyaniline is described. In situ electrochemical surface plasmon resonance (SPR) is used to characterize the bioelectrocatalytic functions of the system.

Aniline Compounds↗