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Electron Transfer Rate (electron + transfer_rate)
Terms modified by Electron Transfer Rate Selected AbstractsSonovoltammetric Elucidation of Electron Transfer Rates: The Oxidation of Dimethyl- p -phenylenediamine in Aqueous SolutionELECTROANALYSIS, Issue 4 2003Craig Abstract The electrochemical oxidation of dimethyl- p -phenylenediamine (DMPD) in aqueous solution (pH 7 phosphate buffer) has been studied under conventional hydrodynamic and microelectrode voltammetric conditions and found to undergo a two-electron electrochemically reversible oxidation. Upon the application of ultrasound to the system an observed shoulder emerges in the oxidation wave. This effect has been attributed to the resolution of the two-electron transfer processes occurring: the first a relatively fast electron transfer (0.1,cm s,1) followed by a second slower (10,3 cm s,1) electron transfer: under the very high mass transport rates induced by insonation an overpotential develops for the second electron transfer so leading to the observed voltammetric resolution. The range of mass transport conditions accessible via sonication allows the estimation of the two rate constants reported. [source] Development of a Glucose Biosensor Using Advanced Electrode Modified by Nanohybrid Composing Chemically Modified Graphene and Ionic LiquidELECTROANALYSIS, Issue 11 2010Ho Yang Abstract Nanohybrids of chemically modified graphene (CMG) and ionic liquid (IL) were prepared by sonication to modify the electrode. The modified CMG-IL electrodes showed a higher current and smaller peak-to-peak potential separation than a bare electrode due to the promoted electron transfer rate. Furthermore, the glucose oxidase (GOx) immobilized on the modified electrode displayed direct electron transfer rate and symmetrical redox potentials with a linear relationship at different scan rates. The fabricated GOx/CMG-IL electrodes were developed selective glucose biosensor with respect to a sensitivity of 0.64,,A mM,1, detection limit of 0.376,mM, and response time of <5,s. [source] Influence of Metal Nanoparticles on the Electrocatalytic Oxidation of Glucose by Poly(NiIIteta) Modified ElectrodesELECTROANALYSIS, Issue 5 2010Pratap Azad Abstract Conductive polymeric [NiII(teta)]2+ (teta=C-meso-5,5,7,12,12,14-hexamethyl-1,4,8,11-tetra-azacyclotetradecane) films (poly(Ni)) have been deposited on the surface of glassy carbon (GC), Nafion (Nf) modified GC (GC/Nf) and Nf stabilized Ag and Au nanoparticles (NPs) modified GC (GC/Ag-Nf and GC/Au-Nf) electrodes. The cyclic voltammogram of the resulting electrodes, show a well defined redox peak due to oxidation and reduction of poly(Ni) system in 0.1,M NaOH. They show electrocatalytic activity towards the oxidation of glucose. AFM studies reveal the formation of poly(Ni) film on the modified electrodes. Presence of metal NPs increases electron transfer rate and electrocatalytic oxidation current by improving the communication within the Nf and poly(Ni) films. In the presence of metal NPs, 4 fold increase in current for glucose oxidation was observed. [source] Ordered Mesoporous Carbon Functionalized with Polythionine for Electrocatalytic ApplicationELECTROANALYSIS, Issue 7 2009Bin Qi Abstract A polythionine (PTH) functionalized ordered mesoporous carbon (OMC) material (PTH/OMC) was presented. The electrochemistry kinetic characteristics of this material are investigated and compared with pure OMC. The results showed that compared with OMC, PTH/OMC possesses a much higher electron transfer rate. For the application of this material, an electrocatalytic based NADH biosensor was constructed on glassy carbon electrode (GCE). Instead of 0.592,V on bare GCE and 0.206,V on OMC/GCE, the amperometric detection of NADH could be effectively performed on the present biosensor with operation potential be set at 0.0,V. In addition, the sensor showed good reproducibility and stability. [source] TEMPERATURE INDUCED PHOTOINHIBITION IN OUTDOOR CULTURES OF MONODUS SUBTERRANEUSJOURNAL OF PHYCOLOGY, Issue 2000A. Vonshak Outdoor algal cultures are continuously exposed to changes in environmental conditions, particularly irradiance and temperature. While the changes in light intensity take place in a range of one to two hours, the increase in temperature is a slower process and takes about four to five hours. This de-synchronization between the two important environmental factors governing photosynthesis and growth of algae results in a unique stress condition where photoinhibition can be induced at relatively low light intensity. Outdoors the early morning culture temperature was found to be about 12 to 14° C, and reaches 25 to 28° C at mid-day. In an experiment, such a natural temperature regime was compared to another one in which the morning temperature of the culture was increased to 20° C by using a heating system. A fast decline in the maximal photochemical efficiency of PSII (Fv/Fm) was observed starting as soon as sunrise. The decline was faster in the non-heated culture and was to a lower value. The diurnal changes in the electron transfer rate (ETR) and in the non-photochemical quenching (NPQ) of the cultures, indicated that the early morning exposure of cells to sub-optimal temperature results in a fast inactivation of PSII activity which was reflected in an inhibition of the photosynthetic activity even when the two cultures finally reached the same temperature at mid-day. Thus, under the same light and temperature mid-day conditions the ETR was higher and the NPQ was significantly lower in the heated culture. Significant changes in productivity of the cultures also were observed. [source] Single-Step Electron Transfer on the Nanometer Scale: Ultra-Fast Charge Shift in Strongly Coupled Zinc Porphyrin,Gold Porphyrin DyadsCHEMISTRY - A EUROPEAN JOURNAL, Issue 11 2008Jérôme Fortage Dr. Abstract The synthesis, electrochemical properties, and photoinduced electron transfer processes of a series of three novel zinc(II),gold(III) bisporphyrin dyads (ZnPSAuP+) are described. The systems studied consist of two trisaryl porphyrins connected directly in the meso position via an alkyne unit to tert -(phenylenethynylene) or penta(phenylenethynylene) spacers. In these dyads, the estimated center to center interporphyrin separation distance varies from 32 to 45,Å. The absorption, emission, and electrochemical data indicate that there are strong electronic interactions between the linked elements, thanks to the direct attachment of the spacer on the porphyrin ring through the alkyne unit. At room temperature in toluene, light excitation of the zinc porphyrin results in almost quantitative formation of the charge shifted state .+ZnPSAuP., whose lifetime is in the order of hundreds of picoseconds. In this solvent, the charge-separated state decays to the ground state through the intermediate population of the zinc porphyrin triplet excited state. Excitation of the gold porphyrin leads instead to rapid energy transfer to the triplet ZnP. In dichloromethane the charge shift reactions are even faster, with time constants down to 2,ps, and may be induced also by excitation of the gold porphyrin. In this latter solvent, the longest charge-shifted lifetime (,=2.3,ns) was obtained with the penta-(phenylenethynylene) spacer. The charge shift reactions are discussed in terms of bridge-mediated super-exchange mechanisms as electron or hole transfer. These new bis-porphyrin arrays, with strong electronic coupling, represent interesting molecular systems in which extremely fast and efficient long-range photoinduced charge shift occurs over a long distance. The rate constants are two to three orders of magnitude larger than for corresponding ZnPAuP+ dyads linked via meso -phenyl groups to oligo-phenyleneethynylene spacers. This study demonstrates the critical impact of the attachment position of the spacer on the porphyrin on the electron transfer rate, and this strategy can represent a useful approach to develop molecular photonic devices for long-range charge separations. [source] Selective Voltammetric Determination of Uric Acid in the Presence of Ascorbic Acid at Ordered Mesoporous Carbon Modified ElectrodesCHINESE JOURNAL OF CHEMISTRY, Issue 6 2008Yan-Li WEN Abstract A novel chemically modified electrode was fabricated by immobilizing ordered mesoporous carbon (OMC) onto a glassy carbon (GC) electrode. The electrocatalytic behavior of the OMC modified electrode towards the oxidation of uric acid (UA) and ascorbic acid (AA) was studied. Compared to a glassy carbon electrode, the OMC modified electrode showed a faster electron transfer rate and reduced the overpotentials greatly. Furthermore, the OMC modified electrode resolved the overlapping voltammetric responses of UA and AA into two well-defined voltammetric peaks with peak separation of ca. 0.38 V. All results show that the OMC modified electrode has a good electrocatalytic ability to UA and AA, and has an excellent response towards UA even in the presence of high concentration AA. [source] Proline-40 is Essential to Maintaining Cytochrome b5, s Stability and Its Electron Transfer with Cytochrome cCHINESE JOURNAL OF CHEMISTRY, Issue 11 2002Zhi-Qian Wang Abstract In order to illustrate the roles played by Pro40 in the structure, properties and functions of Cytochrome b5, three mutated genes, P40V, P40Y, P40G were constructed in this work. Only the P40V gene was successfully expressed into holoprotein in E. coli JM83. According to the results of X-ray crystallographic analysis and various kinds of spectroscopy studies, it is evident that substituting valine for Pro40 does not result in significant alterations in the protein,s overall structure; however, local conformational perturbations in the proximity of the heme do occur. The redox potential of the P40V mutant is 40 mV lower than that of the wild type protein. Its stability towards heat, urea, acid and ethanol were significantly decreased. The mutation leads to a decrease in the hydrophobicity of the heme pocket, which is probably the major factor contributing to the above changes. Binding constants and electron transfer rates between cytochrome bs and cytochrome c were determined using UV-visible spectroscopy and stopped-flow techniques for both the wild type and the mutant. The results showed that the substitution of Pro40 by valine does not influence the binding constant of cytochrome b5 to cytochrome c; however, the electron transfer rate between them decreased significantly. This indicates that proline-40 is essential to maintaining cytochrome bss stability and its electron transfer with cytochrome c. These studies also provided a good example that property and functional changes of a protein do not necessarily require large overall structural alterations; in most cases, only perturbations on the local conformations are sufficient to induce significant changes in protein,s properties and functions. [source] Studies of electron transfer dynamics in particle-surface interactionsISRAEL JOURNAL OF CHEMISTRY, Issue 1-2 2005Vladimir A. EsaulovArticle first published online: 10 MAR 2010 A review of recent work on electron transfer processes leading to neutralization of positive ions and formation of negative ions is presented. Experiments were performed on simple jellium-like metal surfaces, transition metals, and specific characteristics of electronic band structure were investigated for some cases, revealing differences in electron transfer processes between surfaces of the same element. It was shown that electronegative adsorbates like oxygen and chlorine provoke strong changes in electron transfer rates, which are akin to promotion and poisoning of reactions at surfaces. The results of experiments on Auger neutralization of He+ ions on Ag surfaces and H, and F, formation on Ag and Pd surfaces are presented and compared with recent theoretical treatments of these processes. The effect of adsorbates is illustrated by the example of chlorine adsorption on silver. Directions where further theoretical effort would considerably advance the understanding of these phenomena are delineated. [source] Proline-40 is Essential to Maintaining Cytochrome b5, s Stability and Its Electron Transfer with Cytochrome cCHINESE JOURNAL OF CHEMISTRY, Issue 11 2002Zhi-Qian Wang Abstract In order to illustrate the roles played by Pro40 in the structure, properties and functions of Cytochrome b5, three mutated genes, P40V, P40Y, P40G were constructed in this work. Only the P40V gene was successfully expressed into holoprotein in E. coli JM83. According to the results of X-ray crystallographic analysis and various kinds of spectroscopy studies, it is evident that substituting valine for Pro40 does not result in significant alterations in the protein,s overall structure; however, local conformational perturbations in the proximity of the heme do occur. The redox potential of the P40V mutant is 40 mV lower than that of the wild type protein. Its stability towards heat, urea, acid and ethanol were significantly decreased. The mutation leads to a decrease in the hydrophobicity of the heme pocket, which is probably the major factor contributing to the above changes. Binding constants and electron transfer rates between cytochrome bs and cytochrome c were determined using UV-visible spectroscopy and stopped-flow techniques for both the wild type and the mutant. The results showed that the substitution of Pro40 by valine does not influence the binding constant of cytochrome b5 to cytochrome c; however, the electron transfer rate between them decreased significantly. This indicates that proline-40 is essential to maintaining cytochrome bss stability and its electron transfer with cytochrome c. These studies also provided a good example that property and functional changes of a protein do not necessarily require large overall structural alterations; in most cases, only perturbations on the local conformations are sufficient to induce significant changes in protein,s properties and functions. [source] Structures of Cytochrome b5 Mutated at the Charged Surface-Residues and Their Interactions with Cytochrome c,CHINESE JOURNAL OF CHEMISTRY, Issue 11 2002Jlan Wu Abstract Glu44, Glu48, Ghi56 and Asp60 are the negatively charged residues located at the molecular surface of cytochrome b5. Two mutants of cytochrome b5 were prepared, in which two or all of these four residues were mutated to alanines. The mutations give rise to slightly positive shifts of the redox potentials of cytochrome b5 and obvious decrease of the cytochrome b5 -cytochrome c binding constants and electron transfer rates. The crystal structures of the two mutants were determined at 0.18 nm resolution, showing no alteration in overall structures and exhibiting slight changes in the local conformations around the mutation sites as compared with the wild-type protein. Based on the crystal structure of the quadruple-site mutant, a model for the binding of this mutant with cytochrome c is proposed, which involves the salt bridges from Glu37, Glu38 and heme propionate of cytochrome b5 to three lysines of cytochrome c and can well account for the properties and behaviors of this mutant. [source] | ||||||||||