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Long tethers binding redox centers to polymer backbones enhance electron transport in enzyme "Wiring" hydrogels
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Mao F., Mano N., and Heller A. Long tethers binding redox centers to polymer backbones enhance electron transport in enzyme "Wiring" hydrogels. J Am Chem Soc 125 (2003) 4951-4957
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A four-electron O2-electroreduction biocatalyst superior to platinum and a biofuel cell operating at 0.88 V
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The greatest source of inefficiency in the most commonly used acid electrolyte fuel cells, in which either hydrogen or methanol is reacted with oxygen, is the sluggish kinetics of the four-electron electroreduction of oxygen to water on their platinum or platinum alloy catalysts. Reduction of this loss of power and energy is a major thrust of ongoing fuel cell research. This Communication shows that the kinetics of oxygen electroreduction on a carbon electrode coated with an electrocatalyst formed by electrically wiring laccase in a redox hydrogel is so fast that the kinetic loss, termed polarization by electrochemists, is only a fifth of that of platinum.
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Soukharev V., Mano N., and Heller A. A four-electron O2-electroreduction biocatalyst superior to platinum and a biofuel cell operating at 0.88 V. J Am Chem Soc 126 (2004) 8368-8369. The greatest source of inefficiency in the most commonly used acid electrolyte fuel cells, in which either hydrogen or methanol is reacted with oxygen, is the sluggish kinetics of the four-electron electroreduction of oxygen to water on their platinum or platinum alloy catalysts. Reduction of this loss of power and energy is a major thrust of ongoing fuel cell research. This Communication shows that the kinetics of oxygen electroreduction on a carbon electrode coated with an electrocatalyst formed by electrically wiring laccase in a redox hydrogel is so fast that the kinetic loss, termed polarization by electrochemists, is only a fifth of that of platinum.
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On the parameters affecting the characteristics of the "wired" glucose oxidase anode
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Mano N., Mao F., and Heller A. On the parameters affecting the characteristics of the "wired" glucose oxidase anode. J Electroanal Chem 574 (2005) 347-357
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A laccase-wiring redox hydrogel for efficient catalysis of O2 electroreduction
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Mano N., Soukharev V., and Heller A. A laccase-wiring redox hydrogel for efficient catalysis of O2 electroreduction. J Phys Chem B 110 (2006) 11180-11187
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Stabilization of wired glucose oxidase anodes rotating at 1000 rpm at 37 °C
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Binyamin G., and Heller A. Stabilization of wired glucose oxidase anodes rotating at 1000 rpm at 37 °C. J Electrochem Soc 146 (1999) 2965-2967
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Electrodeposition of redox polymers and co-electrodeposition of enzymes by coordinative crosslinking
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Gao Z., Binyamin G., Kim H.-H., Barton S.C., Zhang Y., and Heller A. Electrodeposition of redox polymers and co-electrodeposition of enzymes by coordinative crosslinking. Angew Chem Int Ed 41 (2002) 810-813
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Electrochemical parametrization of metal complex redox potentials, using the ruthenium(III)/ruthenium(II) couple to generate a ligand electrochemical series
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Heller A. Implanted electrochemical glucose sensors for the management of diabetes. Annu Rev Biomed Eng 1 (1999) 153-175
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Heller A. Integrated medical feedback systems for drug delivery. AIChE J 51 (2005) 1054-1066
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24
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21544465904
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Tobacco peroxidase as a new reagent for amperometric biosensors
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Many assays, including affinity and glucose assays, utilize horseradish peroxidase for detecting substrate reaction produced hydrogen peroxide. Electrical connection, or wiring, of the reaction centers of peroxidases to gold or carbon electrodes through redox hydrogels allows monitoring of the hydrogen peroxide concentration as an electrical current. This paper shows that redox hydrogel-wired anionic tobacco peroxidase can be used over a wider pH range and is more stable to inactivation by hydrogen peroxide.
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Gazaryan I.G., Gorton L., Ruzgas T., Csoregi E., Schuhmann W., Lagrimini L.M., Khushpul'yan D.M., and Tishkov V.I. Tobacco peroxidase as a new reagent for amperometric biosensors. J Anal Chem 60 (2005) 558-566. Many assays, including affinity and glucose assays, utilize horseradish peroxidase for detecting substrate reaction produced hydrogen peroxide. Electrical connection, or wiring, of the reaction centers of peroxidases to gold or carbon electrodes through redox hydrogels allows monitoring of the hydrogen peroxide concentration as an electrical current. This paper shows that redox hydrogel-wired anionic tobacco peroxidase can be used over a wider pH range and is more stable to inactivation by hydrogen peroxide.
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J Anal Chem
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Gazaryan, I.G.1
Gorton, L.2
Ruzgas, T.3
Csoregi, E.4
Schuhmann, W.5
Lagrimini, L.M.6
Khushpul'yan, D.M.7
Tishkov, V.I.8
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25
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31044435107
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Miniaturized one-chip electrochemical sensing device integrated with a dialysis membrane and double thin-layer flow channels for measuring blood samples
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Kurita R., Yabumoto N., and Niwa O. Miniaturized one-chip electrochemical sensing device integrated with a dialysis membrane and double thin-layer flow channels for measuring blood samples. Biosens Bioelectron 21 (2006) 1649-1653
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Kurita, R.1
Yabumoto, N.2
Niwa, O.3
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26
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33751509850
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Clarke WL: New study assesses accuracy of Abbott's Investigational FreeStyle Navigator™ continuous glucose monitoring system. In 66th Annual Scientific Sessions of the American Diabetes Association. Washington, DC; 2006. http://www.abbott.com/global/url/pressRelease/en_US/60.5:5/Press_ Release_0325.htm.
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33751516331
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Anon: Abbott's Investigational FreeStyle Navigator™ continuous glucose monitoring system shows promise in two new studies: http://www.abbott.com/global/url/pressRelease/en_US/60.5:5/Press_ Release_0324.htm.
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0346850034
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Oxygen is electroreduced to water on a "wired" enzyme electrode at a lesser overpotential than on platinum
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Mano N., Fernandez J.L., Kim Y., Shin W., Bard A.J., and Heller A. Oxygen is electroreduced to water on a "wired" enzyme electrode at a lesser overpotential than on platinum. J Am Chem Soc 125 (2003) 15290-15291
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Mano, N.1
Fernandez, J.L.2
Kim, Y.3
Shin, W.4
Bard, A.J.5
Heller, A.6
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29
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20344407803
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Mediated biocatalytic cathode for direct methanol membrane-electrode assemblies in biofuel cells
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Hudak N.S., and Barton S.C. Mediated biocatalytic cathode for direct methanol membrane-electrode assemblies in biofuel cells. J Electrochem Soc 152 (2005) A876-A881
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J Electrochem Soc
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Hudak, N.S.1
Barton, S.C.2
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30
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33646230567
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Methanol tolerance of a mediated, biocatalytic oxygen cathode
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Small-sized methanol-air fuel cells with acid electrolytes are currently being investigated as power sources for laptop computers and cell phones. Because methanol oxidation products deactivate the platinum alloy catalyst of their oxygen electroreducing cathodes, methanol must be excluded from the cathode compartment. This is only imperfectly achieved by separation of the anode and cathode compartments with a Nafion membrane. This paper shows that, unlike platinum and its alloys, the redox hydrogel wired laccase electrode is not deactivated by methanol or its oxidation products.
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Sun Y., and Calabrese Barton S. Methanol tolerance of a mediated, biocatalytic oxygen cathode. J Electroanal Chem 590 (2006) 57-65. Small-sized methanol-air fuel cells with acid electrolytes are currently being investigated as power sources for laptop computers and cell phones. Because methanol oxidation products deactivate the platinum alloy catalyst of their oxygen electroreducing cathodes, methanol must be excluded from the cathode compartment. This is only imperfectly achieved by separation of the anode and cathode compartments with a Nafion membrane. This paper shows that, unlike platinum and its alloys, the redox hydrogel wired laccase electrode is not deactivated by methanol or its oxidation products.
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(2006)
J Electroanal Chem
, vol.590
, pp. 57-65
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Sun, Y.1
Calabrese Barton, S.2
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31
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10844225312
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A miniature membrane-less biofuel cell operating at +0.60 V under physiological conditions
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Mano N., Mao F., and Heller A. A miniature membrane-less biofuel cell operating at +0.60 V under physiological conditions. ChemBioChem 5 (2004) 1703-1705
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(2004)
ChemBioChem
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, pp. 1703-1705
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Mano, N.1
Mao, F.2
Heller, A.3
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0038513973
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Characteristics of a miniature compartment-less glucose-O2 biofuel cell and its operation in a living plant
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Mano N., Mao F., and Heller A. Characteristics of a miniature compartment-less glucose-O2 biofuel cell and its operation in a living plant. J Am Chem Soc 125 (2003) 6588-6594
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(2003)
J Am Chem Soc
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, pp. 6588-6594
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Mano, N.1
Mao, F.2
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33
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0037458839
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A miniature biofuel cell operating at 0.78 V
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Mano N., Mao F., Shin W., Chen T., and Heller A. A miniature biofuel cell operating at 0.78 V. Chem Comm (2003) 518-519
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(2003)
Chem Comm
, pp. 518-519
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Mano, N.1
Mao, F.2
Shin, W.3
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Heller, A.5
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34
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0742304946
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Miniature biofuel cells
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2 to water. The cells are the smallest fuel cells ever built.
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2 to water. The cells are the smallest fuel cells ever built.
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(2004)
Phys Chem Chem Phys
, vol.6
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Heller, A.1
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35
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6344276851
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Electro-oxidation of glucose at an increased current density at a reducing potential
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-2 in a physiological buffer solution at 37 °C.
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-2 in a physiological buffer solution at 37 °C.
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(2004)
Chemical Comm
, pp. 2116-2117
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Mano, N.1
Mao, F.2
Heller, A.3
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36
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Potentially implantable miniature batteries
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2 in the subcutaneous fluid would be electroreduced to water on its wired bilirubin oxidase cathode.
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Anal Bioanal Chem
, vol.385
, pp. 469-473
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Heller, A.1
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38
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30144444424
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On the stability of the "wired" bilirubin oxidase oxygen cathode in serum
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Kang C., Shin H., and Heller A. On the stability of the "wired" bilirubin oxidase oxygen cathode in serum. Bioelectrochemistry 68 (2006) 22-26
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(2006)
Bioelectrochemistry
, vol.68
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Kang, C.1
Shin, H.2
Heller, A.3
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39
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Bioelectrochemical propulsion
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-1 when the solution contained glucose and the ends of the fiber were coated with redox hydrogel based wired enzyme electrocatalysts. One fiber end was made to electrooxidized glucose, the other to electroreduce O2. The rapid propulsion was caused by the rapid flow of hydrated protons, generated in the oxidation of glucose at one fiber end and their consumption in the reduction of O2 at the other. The flow was rapid at the air-water interface, where the viscous drag was much lower than in the bulk of the solution.
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-1 when the solution contained glucose and the ends of the fiber were coated with redox hydrogel based wired enzyme electrocatalysts. One fiber end was made to electrooxidized glucose, the other to electroreduce O2. The rapid propulsion was caused by the rapid flow of hydrated protons, generated in the oxidation of glucose at one fiber end and their consumption in the reduction of O2 at the other. The flow was rapid at the air-water interface, where the viscous drag was much lower than in the bulk of the solution.
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(2005)
J Am Chem Soc
, vol.127
, pp. 11574-11575
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Mano, N.1
Heller, A.2
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