메뉴 건너뛰기




Volumn 119, Issue 27, 2015, Pages 14900-14910

New Evidence for a Quasi-Simultaneous Proton-Coupled Two-Electron Transfer and Direct Wiring for Glucose Oxidase Captured by the Carbon Nanotube-Polymer Matrix

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; CATALYST ACTIVITY; COPOLYMERS; CYCLIC VOLTAMMETRY; ELECTRODES; ELECTRON TRANSITIONS; GLUCOSE; GLUCOSE OXIDASE; GLUCOSE SENSORS; MATRIX ALGEBRA; NANOTECHNOLOGY; YARN;

EID: 84936864193     PISSN: 19327447     EISSN: 19327455     Source Type: Journal    
DOI: 10.1021/acs.jpcc.5b02796     Document Type: Article
Times cited : (17)

References (67)
  • 2
    • 13444310821 scopus 로고    scopus 로고
    • Glucose Oxidase from Aspergillus Niger: The Mechanism of Action with Molecular Oxygen, Quinones, and One-Electron Acceptors
    • Leskovac, V.; Trivić, S.; Wohlfahrt, G.; Kandrač, J.; Peričin, D. Glucose Oxidase from Aspergillus Niger: The Mechanism of Action with Molecular Oxygen, Quinones, and One-Electron Acceptors Int. J. Biochem. Cell Biol. 2005, 37, 731-750
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 731-750
    • Leskovac, V.1    Trivić, S.2    Wohlfahrt, G.3    Kandrač, J.4    Peričin, D.5
  • 3
    • 49049113124 scopus 로고    scopus 로고
    • Electrochemical Glucose Sensors and Their Applications in Diabetes Management
    • Heller, A.; Feldman, B. Electrochemical Glucose Sensors and Their Applications in Diabetes Management Chem. Rev. 2008, 108, 2482-2505
    • (2008) Chem. Rev. , vol.108 , pp. 2482-2505
    • Heller, A.1    Feldman, B.2
  • 4
    • 0033614811 scopus 로고    scopus 로고
    • Nature of Oxygen Activation in Glucose Oxidase from Aspergillus Niger: The Importance of Electrostatic Stabilization in Superoxide Formation
    • Su, Q.; Klinman, J. P. Nature of Oxygen Activation in Glucose Oxidase from Aspergillus Niger: The Importance of Electrostatic Stabilization in Superoxide Formation Biochemistry 1999, 38, 8572-8581
    • (1999) Biochemistry , vol.38 , pp. 8572-8581
    • Su, Q.1    Klinman, J.P.2
  • 5
    • 0037422546 scopus 로고    scopus 로고
    • Catalysis of Electron Transfer during Activation of O2 by the Flavoprotein Glucose Oxidase
    • Roth, J. P.; Klinman, J. P. Catalysis of Electron Transfer during Activation of O2 by the Flavoprotein Glucose Oxidase Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 62-67
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 62-67
    • Roth, J.P.1    Klinman, J.P.2
  • 6
    • 9444274813 scopus 로고    scopus 로고
    • Oxygen Isotope Effects on Electron Transfer to O2 Probed Using Chemically Modified Flavins Bound to Glucose Oxidase
    • Roth, J. P.; Wincek, R.; Nodet, G.; Edmondson, D. E.; McIntire, W. S.; Klinman, J. P. Oxygen Isotope Effects on Electron Transfer to O2 Probed Using Chemically Modified Flavins Bound to Glucose Oxidase J. Am. Chem. Soc. 2004, 126, 15120-15131
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15120-15131
    • Roth, J.P.1    Wincek, R.2    Nodet, G.3    Edmondson, D.E.4    McIntire, W.S.5    Klinman, J.P.6
  • 7
    • 27844574240 scopus 로고    scopus 로고
    • Determination of a Large Reorganization Energy Barrier for Hydride Abstraction by Glucose Oxidase
    • Brinkley, D. W.; Roth, J. P. Determination of a Large Reorganization Energy Barrier for Hydride Abstraction by Glucose Oxidase J. Am. Chem. Soc. 2005, 127, 15720-15721
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15720-15721
    • Brinkley, D.W.1    Roth, J.P.2
  • 8
    • 0027397187 scopus 로고
    • Crystal Structure of Glucose Oxidase from Aspergillus Niger Refined at 2.3 Å Reslution
    • Hecht, H. J.; Kalisz, H. M.; Hendle, J.; Schmid, R. D.; Schomburg, D. Crystal Structure of Glucose Oxidase from Aspergillus Niger Refined at 2.3 Å Reslution J. Mol. Biol. 1993, 229, 153-172
    • (1993) J. Mol. Biol. , vol.229 , pp. 153-172
    • Hecht, H.J.1    Kalisz, H.M.2    Hendle, J.3    Schmid, R.D.4    Schomburg, D.5
  • 9
    • 0027272553 scopus 로고
    • The 3D Structure of Glucose Oxidase from Aspergillus Niger. Implications for the Use of GOD as a Biosensor Enzyme
    • Hecht, H. J.; Schomburg, D.; Kalisz, H.; Schmid, R. D. The 3D Structure of Glucose Oxidase from Aspergillus Niger. Implications for the Use of GOD as a Biosensor Enzyme Biosens. Bioelectron. 1993, 8, 197-203
    • (1993) Biosens. Bioelectron. , vol.8 , pp. 197-203
    • Hecht, H.J.1    Schomburg, D.2    Kalisz, H.3    Schmid, R.D.4
  • 10
    • 0033135955 scopus 로고    scopus 로고
    • 1.8 and 1.9 Å Resolution Structures of the Penicillium Amagasakiense and Aspergillus Niger Glucose Oxidases as a Basis for Modelling Substrate Complexes
    • Wohlfahrt, G.; Witt, S.; Hendle, J.; Schomburg, D.; Kalisz, H. M.; Hecht, H.-J. 1.8 and 1.9 Å Resolution Structures of the Penicillium Amagasakiense and Aspergillus Niger Glucose Oxidases as a Basis for Modelling Substrate Complexes Acta Crystallogr., Sect. D: Biol. Crystallogr. 1999, 55, 969-977
    • (1999) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.55 , pp. 969-977
    • Wohlfahrt, G.1    Witt, S.2    Hendle, J.3    Schomburg, D.4    Kalisz, H.M.5    Hecht, H.-J.6
  • 11
    • 10844225312 scopus 로고    scopus 로고
    • A Miniature Membrane-Less Biofuel Cell Operating at +0.60 V under Physiological Conditions
    • Mano, N.; Mao, F.; Heller, A. A Miniature Membrane-Less Biofuel Cell Operating at +0.60 V under Physiological Conditions ChemBioChem 2004, 5, 1703-1705
    • (2004) ChemBioChem , vol.5 , pp. 1703-1705
    • Mano, N.1    Mao, F.2    Heller, A.3
  • 12
    • 0036802211 scopus 로고    scopus 로고
    • Direct Electron Transfer of Glucose Oxidase on Carbon Nanotubes
    • Guiseppi-Elie, A.; Lei, C.; Baughman, R. H. Direct Electron Transfer of Glucose Oxidase on Carbon Nanotubes Nanotechnology 2002, 13, 559
    • (2002) Nanotechnology , vol.13 , pp. 559
    • Guiseppi-Elie, A.1    Lei, C.2    Baughman, R.H.3
  • 13
    • 4544315692 scopus 로고    scopus 로고
    • Long-Range Electrical Contacting of Redox Enzymes by SWCNT Connectors
    • Patolsky, F.; Weizmann, Y.; Willner, I. Long-Range Electrical Contacting of Redox Enzymes by SWCNT Connectors Angew. Chem., Int. Ed. 2004, 43, 2113-2117
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 2113-2117
    • Patolsky, F.1    Weizmann, Y.2    Willner, I.3
  • 14
    • 14344257257 scopus 로고    scopus 로고
    • Achieving Direct Electrical Connection to Glucose Oxidase Using Aligned Single Walled Carbon Nanotube Arrays
    • Liu, J.; Chou, A.; Rahmat, W.; Paddon-Row, M. N.; Gooding, J. J. Achieving Direct Electrical Connection to Glucose Oxidase Using Aligned Single Walled Carbon Nanotube Arrays Electroanalysis 2005, 17, 38-46
    • (2005) Electroanalysis , vol.17 , pp. 38-46
    • Liu, J.1    Chou, A.2    Rahmat, W.3    Paddon-Row, M.N.4    Gooding, J.J.5
  • 15
    • 3042545770 scopus 로고    scopus 로고
    • Heterogeneous Electron-Transfer Kinetics for Flavin Adenine Dinucleotide and Ferrocene through Alkanethiol Mixed Monolayers on Gold Electrodes
    • Liu, J.; Paddon-Row, M. N.; Gooding, J. J. Heterogeneous Electron-Transfer Kinetics for Flavin Adenine Dinucleotide and Ferrocene through Alkanethiol Mixed Monolayers on Gold Electrodes J. Phys. Chem. B 2004, 108, 8460-8466
    • (2004) J. Phys. Chem. B , vol.108 , pp. 8460-8466
    • Liu, J.1    Paddon-Row, M.N.2    Gooding, J.J.3
  • 16
    • 84891822540 scopus 로고    scopus 로고
    • On the Direct Electron Transfer, Sensing, and Enzyme Activity in the Glucose Oxidase/Carbon Nanotubes System
    • Wooten, M.; Karra, S.; Zhang, M.; Gorski, W. On the Direct Electron Transfer, Sensing, and Enzyme Activity in the Glucose Oxidase/Carbon Nanotubes System Anal. Chem. 2014, 86, 752-757
    • (2014) Anal. Chem. , vol.86 , pp. 752-757
    • Wooten, M.1    Karra, S.2    Zhang, M.3    Gorski, W.4
  • 17
    • 0242438104 scopus 로고    scopus 로고
    • Voltammetric Simulations of Multiple Electron Transfer/Proton Transfer Coupled Reactions: Flavin Adenine Dinucleotide as a Model System
    • Smith, E. T.; Davis, C. A.; Barber, M. J. Voltammetric Simulations of Multiple Electron Transfer/Proton Transfer Coupled Reactions: Flavin Adenine Dinucleotide as a Model System Anal. Biochem. 2003, 323, 114-121
    • (2003) Anal. Biochem. , vol.323 , pp. 114-121
    • Smith, E.T.1    Davis, C.A.2    Barber, M.J.3
  • 18
    • 17044393894 scopus 로고    scopus 로고
    • Identifying the N = 2 Reaction Mechanism of FAD through Voltammetric Simulations
    • Cable, M.; Smith, E. T. Identifying the N = 2 Reaction Mechanism of FAD through Voltammetric Simulations Anal. Chim. Acta 2005, 537, 299-306
    • (2005) Anal. Chim. Acta , vol.537 , pp. 299-306
    • Cable, M.1    Smith, E.T.2
  • 19
    • 84873333974 scopus 로고    scopus 로고
    • Influence of Surface Adsorption on the Interfacial Electron Transfer of Flavin Adenine Dinucleotide and Glucose Oxidase at Carbon Nanotube and Nitrogen-Doped Carbon Nanotube Electrodes
    • Goran, J. M.; Mantilla, S. M.; Stevenson, K. J. Influence of Surface Adsorption on the Interfacial Electron Transfer of Flavin Adenine Dinucleotide and Glucose Oxidase at Carbon Nanotube and Nitrogen-Doped Carbon Nanotube Electrodes Anal. Chem. 2013, 85, 1571-1581
    • (2013) Anal. Chem. , vol.85 , pp. 1571-1581
    • Goran, J.M.1    Mantilla, S.M.2    Stevenson, K.J.3
  • 20
    • 84897087009 scopus 로고    scopus 로고
    • New Insights into the Analysis of the Electrode Kinetics of Flavin Adenine Dinucleotide Redox Center of Glucose Oxidase Immobilized on Carbon Electrodes
    • Simonov, A. N.; Grosse, W.; Mashkina, E. A.; Bethwaite, B.; Tan, J.; Abramson, D.; Wallace, G. G.; Moulton, S. E.; Bond, A. M. New Insights into the Analysis of the Electrode Kinetics of Flavin Adenine Dinucleotide Redox Center of Glucose Oxidase Immobilized on Carbon Electrodes Langmuir 2014, 30, 3264-3273
    • (2014) Langmuir , vol.30 , pp. 3264-3273
    • Simonov, A.N.1    Grosse, W.2    Mashkina, E.A.3    Bethwaite, B.4    Tan, J.5    Abramson, D.6    Wallace, G.G.7    Moulton, S.E.8    Bond, A.M.9
  • 21
    • 68549123501 scopus 로고    scopus 로고
    • Breaking the Barrier to Fast Electron Transfer
    • Demin, S.; Hall, E. A. H. Breaking the Barrier to Fast Electron Transfer Bioelectrochemistry 2009, 76, 19-27
    • (2009) Bioelectrochemistry , vol.76 , pp. 19-27
    • Demin, S.1    Hall, E.A.H.2
  • 22
    • 58349105346 scopus 로고    scopus 로고
    • Direct Electrochemistry of Glucose Oxidase Immobilized on NdPO4 Nanoparticles/Chitosan Composite Film on Glassy Carbon Electrodes and Its Biosensing Application
    • Sheng, Q.; Luo, K.; Li, L.; Zheng, J. Direct Electrochemistry of Glucose Oxidase Immobilized on NdPO4 Nanoparticles/Chitosan Composite Film on Glassy Carbon Electrodes and Its Biosensing Application Bioelectrochemistry 2009, 74, 246-253
    • (2009) Bioelectrochemistry , vol.74 , pp. 246-253
    • Sheng, Q.1    Luo, K.2    Li, L.3    Zheng, J.4
  • 24
    • 33947338100 scopus 로고
    • Multistep Charge Transfers in Stationary Electrode Polarography
    • Polcyn, D. S.; Shain, I. Multistep Charge Transfers in Stationary Electrode Polarography Anal. Chem. 1966, 38, 370-375
    • (1966) Anal. Chem. , vol.38 , pp. 370-375
    • Polcyn, D.S.1    Shain, I.2
  • 25
    • 0019875765 scopus 로고
    • Electrostatic Control of Enzyme Reactions: Effect of Ionic Strength on the pKa of an Essential Acidic Group on Glucose Oxidase
    • Voet, J. G.; Coe, J.; Epstein, J.; Matossian, V.; Shipley, T. Electrostatic Control of Enzyme Reactions: Effect of Ionic Strength on the pKa of an Essential Acidic Group on Glucose Oxidase Biochemistry 1981, 20, 7182-7185
    • (1981) Biochemistry , vol.20 , pp. 7182-7185
    • Voet, J.G.1    Coe, J.2    Epstein, J.3    Matossian, V.4    Shipley, T.5
  • 26
    • 8344271158 scopus 로고    scopus 로고
    • Probing Electron Tunneling Pathways: Electrochemical Study of Rat Heart Cytochrome C and Its Mutant on Pyridine-Terminated Sams
    • Wei, J. J.; Liu, H.; Niki, K.; Margoliash, E.; Waldeck, D. H. Probing Electron Tunneling Pathways: Electrochemical Study of Rat Heart Cytochrome C and Its Mutant on Pyridine-Terminated Sams J. Phys. Chem. B 2004, 108, 16912-16917
    • (2004) J. Phys. Chem. B , vol.108 , pp. 16912-16917
    • Wei, J.J.1    Liu, H.2    Niki, K.3    Margoliash, E.4    Waldeck, D.H.5
  • 27
    • 36849118773 scopus 로고
    • On the Theory of Electron-Transfer Reactions. VI. Unified Treatment for Homogeneous and Electrode Reactions
    • Marcus, R. A. On the Theory of Electron-Transfer Reactions. VI. Unified Treatment for Homogeneous and Electrode Reactions J. Chem. Phys. 1965, 43, 679-701
    • (1965) J. Chem. Phys. , vol.43 , pp. 679-701
    • Marcus, R.A.1
  • 28
    • 0010047929 scopus 로고
    • Theory of Charge Transfer Kinetics at Solid-Polar Liquid Interfaces
    • Dogonadze, R. R.; Kuznetsov, A. M. Theory of Charge Transfer Kinetics at Solid-Polar Liquid Interfaces Prog. Surf. Sci. 1975, 6, 1-41
    • (1975) Prog. Surf. Sci. , vol.6 , pp. 1-41
    • Dogonadze, R.R.1    Kuznetsov, A.M.2
  • 30
    • 84943503743 scopus 로고
    • Dynamic Solvent Effects in Electron Transfer Reactions
    • Zusman, L. D. Dynamic Solvent Effects in Electron Transfer Reactions Z. Phys. Chem. (Munchen) 1994, 186, 1-29
    • (1994) Z. Phys. Chem. (Munchen) , vol.186 , pp. 1-29
    • Zusman, L.D.1
  • 31
    • 0011526199 scopus 로고    scopus 로고
    • Electron Transfer - From Isolated Molecules to Biomolecules
    • John Wiley & Sons, Inc. New York
    • Bixon, M.; Jortner, J., Electron Transfer-From Isolated Molecules to Biomolecules. In Advances in Chemical Physics; John Wiley & Sons, Inc.: New York, 2007; pp 35-202.
    • (2007) Advances in Chemical Physics , pp. 35-202
    • Bixon, M.1    Jortner, J.2
  • 32
    • 84897987543 scopus 로고    scopus 로고
    • Biochemistry and Theory of Proton-Coupled Electron Transfer
    • Migliore, A.; Polizzi, N. F.; Therien, M. J.; Beratan, D. N. Biochemistry and Theory of Proton-Coupled Electron Transfer Chem. Rev. 2014, 114, 3381-3465
    • (2014) Chem. Rev. , vol.114 , pp. 3381-3465
    • Migliore, A.1    Polizzi, N.F.2    Therien, M.J.3    Beratan, D.N.4
  • 33
    • 21844487229 scopus 로고
    • Dynamics of Low-Barrier Proton Transfer in Polar Solvents and Protein Media
    • Kuznetsov, A. M.; Ulstrup, J. Dynamics of Low-Barrier Proton Transfer in Polar Solvents and Protein Media Chem. Phys. 1994, 188, 131-141
    • (1994) Chem. Phys. , vol.188 , pp. 131-141
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 34
    • 0034640371 scopus 로고    scopus 로고
    • The Mechanism of the Proton Transfer: An Outline
    • Krishtalik, L. I. The Mechanism of the Proton Transfer: An Outline Biochim. Biophys. Acta, Bioenerg. 2000, 1458, 6-27
    • (2000) Biochim. Biophys. Acta, Bioenerg. , vol.1458 , pp. 6-27
    • Krishtalik, L.I.1
  • 35
    • 80053575236 scopus 로고    scopus 로고
    • Diverse Role of Conformational Dynamics in Carboxypeptidase a-Driven Peptide and Ester Hydrolyses: Disclosing the "Perfect Induced Fit" and "Protein Local Unfolding" Pathways by Altering Protein Stability
    • Shushanyan, M.; Khoshtariya, D. E.; Tretyakova, T.; Makharadze, M.; van Eldik, R. Diverse Role of Conformational Dynamics in Carboxypeptidase a-Driven Peptide and Ester Hydrolyses: Disclosing the "Perfect Induced Fit" and "Protein Local Unfolding" Pathways by Altering Protein Stability Biopolymers 2011, 95, 852-870
    • (2011) Biopolymers , vol.95 , pp. 852-870
    • Shushanyan, M.1    Khoshtariya, D.E.2    Tretyakova, T.3    Makharadze, M.4    Van Eldik, R.5
  • 36
    • 0001554306 scopus 로고
    • Voltammetry of Redox-Active Groups Irreversibly Adsorbed onto Electrodes. Treatment Using the Marcus Relation between Rate and Overpotential
    • Weber, K.; Creager, S. E. Voltammetry of Redox-Active Groups Irreversibly Adsorbed onto Electrodes. Treatment Using the Marcus Relation between Rate and Overpotential Anal. Chem. 1994, 66, 3164-3172
    • (1994) Anal. Chem. , vol.66 , pp. 3164-3172
    • Weber, K.1    Creager, S.E.2
  • 37
    • 0031561238 scopus 로고    scopus 로고
    • Long-Range Electronic Coupling between Ferrocene and Gold in Alkanethiolate-Based Monolayers on Electrodes
    • Weber, K.; Hockett, L.; Creager, S. Long-Range Electronic Coupling between Ferrocene and Gold in Alkanethiolate-Based Monolayers on Electrodes J. Phys. Chem. B 1997, 101, 8286-8291
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8286-8291
    • Weber, K.1    Hockett, L.2    Creager, S.3
  • 38
    • 0000486126 scopus 로고
    • Cyclic Voltammetric Analysis of Ferrocene Alkanethiol Monolayer Electrode Kinetics Based on Marcus Theory
    • Tender, L.; Carter, M. T.; Murray, R. W. Cyclic Voltammetric Analysis of Ferrocene Alkanethiol Monolayer Electrode Kinetics Based on Marcus Theory Anal. Chem. 1994, 66, 3173-3181
    • (1994) Anal. Chem. , vol.66 , pp. 3173-3181
    • Tender, L.1    Carter, M.T.2    Murray, R.W.3
  • 39
    • 0035899737 scopus 로고    scopus 로고
    • The Nature of Electronic Coupling between Ferrocene and Gold through Alkanethiolate Monolayers on Electrodes: The Importance of Chain Composition, Interchain Coupling, and Quantum Interference
    • Napper, A. M.; Liu, H.; Waldeck, D. H. The Nature of Electronic Coupling between Ferrocene and Gold through Alkanethiolate Monolayers on Electrodes: The Importance of Chain Composition, Interchain Coupling, and Quantum Interference J. Phys. Chem. B 2001, 105, 7699-7707
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7699-7707
    • Napper, A.M.1    Liu, H.2    Waldeck, D.H.3
  • 40
    • 0242268469 scopus 로고    scopus 로고
    • Nonlinear Elasticity, Proteinquakes, and the Energy Landscapes of Functional Transitions in Proteins
    • Miyashita, O.; Onuchic, J. N.; Wolynes, P. G. Nonlinear Elasticity, Proteinquakes, and the Energy Landscapes of Functional Transitions in Proteins Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 12570-12575
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12570-12575
    • Miyashita, O.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 41
    • 69749119200 scopus 로고    scopus 로고
    • The Spectrum of Biomolecular States and Motions
    • Hegler, J. A.; Weinkam, P.; Wolynes, P. G. The Spectrum of Biomolecular States and Motions HFSP J. 2008, 2, 307-313
    • (2008) HFSP J. , vol.2 , pp. 307-313
    • Hegler, J.A.1    Weinkam, P.2    Wolynes, P.G.3
  • 42
    • 36849074084 scopus 로고    scopus 로고
    • Picosecond Fluctuating Protein Energy Landscape Mapped by Pressure-Temperature Molecular Dynamics Simulation
    • Meinhold, L.; Smith, J. C.; Kitao, A.; Zewail, A. H. Picosecond Fluctuating Protein Energy Landscape Mapped by Pressure-Temperature Molecular Dynamics Simulation Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 17261-17265
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17261-17265
    • Meinhold, L.1    Smith, J.C.2    Kitao, A.3    Zewail, A.H.4
  • 43
    • 42449131294 scopus 로고    scopus 로고
    • Glassy Protein Dynamics and Gigantic Solvent Reorganization Energy of Plastocyanin
    • LeBard, D. N.; Matyushov, D. V. Glassy Protein Dynamics and Gigantic Solvent Reorganization Energy of Plastocyanin J. Phys. Chem. B 2008, 112, 5218-5227
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5218-5227
    • Lebard, D.N.1    Matyushov, D.V.2
  • 44
    • 80052521875 scopus 로고    scopus 로고
    • Nanosecond Stokes Shift Dynamics, Dynamical Transition, and Gigantic Reorganization Energy of Hydrated Heme Proteins
    • Matyushov, D. V. Nanosecond Stokes Shift Dynamics, Dynamical Transition, and Gigantic Reorganization Energy of Hydrated Heme Proteins J. Phys. Chem. B 2011, 115, 10715-10724
    • (2011) J. Phys. Chem. B , vol.115 , pp. 10715-10724
    • Matyushov, D.V.1
  • 45
    • 84930505290 scopus 로고    scopus 로고
    • Electron Transfer with Copper Ions Self-Assembled at Au-Deposited Biomimetic Films: Mechanistic "Anomalies" Disclosed by Temperature- and Pressure-Assisted Fast-Scan Voltammetry
    • 11p
    • Khoshtariya, D. E.; Dolidze, T. D.; Tretyakova, T.; van Eldik, R. Electron Transfer with Copper Ions Self-Assembled at Au-Deposited Biomimetic Films: Mechanistic "Anomalies" Disclosed by Temperature- and Pressure-Assisted Fast-Scan Voltammetry J. Phys. D: Appl. Phys. 2015, 48, 255402 (11p)
    • (2015) J. Phys. D: Appl. Phys. , vol.48 , pp. 255402
    • Khoshtariya, D.E.1    Dolidze, T.D.2    Tretyakova, T.3    Van Eldik, R.4
  • 46
    • 84884339806 scopus 로고    scopus 로고
    • Electron Transfer with Azurin at Au-SAM Junctions in Contact with a Protic Ionic Melt: Impact of Glassy Dynamics
    • Khoshtariya, D. E.; Dolidze, T. D.; Tretyakova, T.; Waldeck, D. H.; van Eldik, R. Electron Transfer with Azurin at Au-SAM Junctions in Contact with a Protic Ionic Melt: Impact of Glassy Dynamics Phys. Chem. Chem. Phys. 2013, 15, 16515-16526
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 16515-16526
    • Khoshtariya, D.E.1    Dolidze, T.D.2    Tretyakova, T.3    Waldeck, D.H.4    Van Eldik, R.5
  • 47
    • 0038877802 scopus 로고
    • Phase-Integral Calculation of the Energy Levels of a Quantal Anharmonic Oscillator
    • Lakshmanan, M.; Karlsson, F.; Fröman, P. O. Phase-Integral Calculation of the Energy Levels of a Quantal Anharmonic Oscillator Phys. Rev. D 1981, 24, 2586-2598
    • (1981) Phys. Rev. D , vol.24 , pp. 2586-2598
    • Lakshmanan, M.1    Karlsson, F.2    Fröman, P.O.3
  • 48
    • 34547824542 scopus 로고
    • Energy Levels of the Quartic Double Well Using a Phase-Integral Method
    • Yuste, S. B.; Sánchez, A. M. Energy Levels of the Quartic Double Well Using a Phase-Integral Method Phys. Rev. A 1993, 48, 3478-3485
    • (1993) Phys. Rev. A , vol.48 , pp. 3478-3485
    • Yuste, S.B.1    Sánchez, A.M.2
  • 49
    • 0037122125 scopus 로고    scopus 로고
    • Electron-Transfer Dynamics of Cytochrome C: A Change in the Reaction Mechanism with Distance
    • Wei, J.; Liu, H.; Khoshtariya, D. E.; Yamamoto, H.; Dick, A.; Waldeck, D. H. Electron-Transfer Dynamics of Cytochrome C: A Change in the Reaction Mechanism with Distance Angew. Chem., Int. Ed. 2002, 41, 4700-4703
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 4700-4703
    • Wei, J.1    Liu, H.2    Khoshtariya, D.E.3    Yamamoto, H.4    Dick, A.5    Waldeck, D.H.6
  • 50
    • 0038546674 scopus 로고    scopus 로고
    • Charge-Transfer Mechanism for Cytochrome C Adsorbed on Nanometer Thick Films. Distinguishing Frictional Control from Conformational Gating
    • Khoshtariya, D. E.; Wei, J.; Liu, H.; Yue, H.; Waldeck, D. H. Charge-Transfer Mechanism for Cytochrome C Adsorbed on Nanometer Thick Films. Distinguishing Frictional Control from Conformational Gating J. Am. Chem. Soc. 2003, 125, 7704-7714
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7704-7714
    • Khoshtariya, D.E.1    Wei, J.2    Liu, H.3    Yue, H.4    Waldeck, D.H.5
  • 51
    • 29544432512 scopus 로고    scopus 로고
    • High-Pressure Probing of a Changeover in the Charge-Transfer Mechanism for Intact Cytochrome C at Gold/Self-Assembled Monolayer Junctions
    • Khoshtariya, D. E.; Dolidze, T. D.; Sarauli, D.; van Eldik, R. High-Pressure Probing of a Changeover in the Charge-Transfer Mechanism for Intact Cytochrome C at Gold/Self-Assembled Monolayer Junctions Angew. Chem., Int. Ed. 2006, 45, 277-281
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 277-281
    • Khoshtariya, D.E.1    Dolidze, T.D.2    Sarauli, D.3    Van Eldik, R.4
  • 52
    • 33749000335 scopus 로고    scopus 로고
    • Kinetic, Thermodynamic, and Mechanistic Patterns for Free (Unbound) Cytochrome C at Au/SAM Junctions: Impact of Electronic Coupling, Hydrostatic Pressure, and Stabilizing/Denaturing Additives
    • Khoshtariya, D. E.; Dolidze, T. D.; Seifert, S.; Sarauli, D.; Lee, G.; van Eldik, R. Kinetic, Thermodynamic, and Mechanistic Patterns for Free (Unbound) Cytochrome C at Au/SAM Junctions: Impact of Electronic Coupling, Hydrostatic Pressure, and Stabilizing/Denaturing Additives Chem.-Eur. J. 2006, 12, 7007-7007
    • (2006) Chem. - Eur. J. , vol.12 , pp. 7007-7007
    • Khoshtariya, D.E.1    Dolidze, T.D.2    Seifert, S.3    Sarauli, D.4    Lee, G.5    Van Eldik, R.6
  • 53
  • 54
    • 34548651723 scopus 로고    scopus 로고
    • Impact of Self-Assembly Composition on the Alternate Interfacial Electron Transfer for Electrostatically Immobilized Cytochrome
    • Dolidze, T. D.; Rondinini, S.; Vertova, A.; Waldeck, D. H.; Khoshtariya, D. E. Impact of Self-Assembly Composition on the Alternate Interfacial Electron Transfer for Electrostatically Immobilized Cytochrome C. Biopolymers 2007, 87, 68-73
    • (2007) C. Biopolymers , vol.87 , pp. 68-73
    • Dolidze, T.D.1    Rondinini, S.2    Vertova, A.3    Waldeck, D.H.4    Khoshtariya, D.E.5
  • 55
    • 84893132050 scopus 로고    scopus 로고
    • Long-Range Electron Transfer with Myoglobin Immobilized at Au/Mixed-SAM Junctions: Mechanistic Impact of the Strong Protein Confinement
    • Khoshtariya, D. E.; Dolidze, T. D.; Shushanyan, M.; van Eldik, R. Long-Range Electron Transfer with Myoglobin Immobilized at Au/Mixed-SAM Junctions: Mechanistic Impact of the Strong Protein Confinement J. Phys. Chem. B 2014, 118, 692-706
    • (2014) J. Phys. Chem. B , vol.118 , pp. 692-706
    • Khoshtariya, D.E.1    Dolidze, T.D.2    Shushanyan, M.3    Van Eldik, R.4
  • 56
    • 0029166546 scopus 로고
    • Improving Enzyme Electrode Contacts by Redox Modification of Cofactors
    • Riklin, A.; Katz, E.; Willner, I.; Stocker, A.; Bückmann, A. F. Improving Enzyme Electrode Contacts by Redox Modification of Cofactors Nature 1995, 376, 672-675
    • (1995) Nature , vol.376 , pp. 672-675
    • Riklin, A.1    Katz, E.2    Willner, I.3    Stocker, A.4    Bückmann, A.F.5
  • 57
    • 34547939432 scopus 로고    scopus 로고
    • A Molecular Wire Modified Glassy Carbon Electrode for Achieving Direct Electron Transfer to Native Glucose Oxidase
    • Liu, G.; Paddon-Row, M. N.; Gooding, J. J. A Molecular Wire Modified Glassy Carbon Electrode for Achieving Direct Electron Transfer to Native Glucose Oxidase Electrochem. Commun. 2007, 9, 2218-2223
    • (2007) Electrochem. Commun. , vol.9 , pp. 2218-2223
    • Liu, G.1    Paddon-Row, M.N.2    Gooding, J.J.3
  • 58
    • 75749089928 scopus 로고    scopus 로고
    • Direct Electron Transfer and Conformational Change of Glucose Oxidase on Carbon Nanotube-Based Electrodes
    • Zhao, H.-Z.; Sun, J.-J.; Song, J.; Yang, Q.-Z. Direct Electron Transfer and Conformational Change of Glucose Oxidase on Carbon Nanotube-Based Electrodes Carbon 2010, 48, 1508-1514
    • (2010) Carbon , vol.48 , pp. 1508-1514
    • Zhao, H.-Z.1    Sun, J.-J.2    Song, J.3    Yang, Q.-Z.4
  • 59
    • 0038451398 scopus 로고    scopus 로고
    • Gold Electrodes Wired for Coupling with the Deeply Buried Active Site of Arthrobacter Globiformis Amine Oxidase
    • Hess, C. R.; Juda, G. A.; Dooley, D. M.; Amii, R. N.; Hill, M. G.; Winkler, J. R.; Gray, H. B. Gold Electrodes Wired for Coupling with the Deeply Buried Active Site of Arthrobacter Globiformis Amine Oxidase J. Am. Chem. Soc. 2003, 125, 7156-7157
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7156-7157
    • Hess, C.R.1    Juda, G.A.2    Dooley, D.M.3    Amii, R.N.4    Hill, M.G.5    Winkler, J.R.6    Gray, H.B.7
  • 60
    • 77649312913 scopus 로고    scopus 로고
    • Direct Electrochemistry of Glucose Oxidase on Nail-Like Carbon and Its Biosensing for Glucose
    • Li, K.; Liu, B.; Zheng, J.; Sheng, Q.; Liu, R. Direct Electrochemistry of Glucose Oxidase on Nail-Like Carbon and Its Biosensing for Glucose Electroanalysis 2010, 22, 701-706
    • (2010) Electroanalysis , vol.22 , pp. 701-706
    • Li, K.1    Liu, B.2    Zheng, J.3    Sheng, Q.4    Liu, R.5
  • 61
    • 0023828799 scopus 로고
    • The Electrochemical Behavior of Flavin Adenine Dinucleotide in Neutral Solutions
    • Birss, V. I.; Elzanowska, H.; Turner, R. A. The Electrochemical Behavior of Flavin Adenine Dinucleotide in Neutral Solutions Can. J. Chem. 1988, 66, 86-96
    • (1988) Can. J. Chem. , vol.66 , pp. 86-96
    • Birss, V.I.1    Elzanowska, H.2    Turner, R.A.3
  • 62
    • 33845287671 scopus 로고    scopus 로고
    • Enzymatic Catalysis and Transfers in Solution. I. Theory and Computations, a Unified View
    • Marcus, R. A. Enzymatic Catalysis and Transfers in Solution. I. Theory and Computations, a Unified View J. Chem. Phys. 2006, 125, 194504
    • (2006) J. Chem. Phys. , vol.125 , pp. 194504
    • Marcus, R.A.1
  • 64
    • 0037041566 scopus 로고    scopus 로고
    • Two-Electron Transfer for Tl(Aq)3+/Tl(Aq)+ Revisited. Common Virtual [TlII-TlII]4+ Intermediate for Homogeneous (Superexchange) and Electrode (Sequential) Mechanisms
    • Khoshtariya, D. E.; Dolidze, T. D.; Zusman, L. D.; Lindbergh, G.; Glaser, J. Two-Electron Transfer for Tl(Aq)3+/Tl(Aq)+ Revisited. Common Virtual [TlII-TlII]4+ Intermediate for Homogeneous (Superexchange) and Electrode (Sequential) Mechanisms Inorg. Chem. 2002, 41, 1728-1738
    • (2002) Inorg. Chem. , vol.41 , pp. 1728-1738
    • Khoshtariya, D.E.1    Dolidze, T.D.2    Zusman, L.D.3    Lindbergh, G.4    Glaser, J.5
  • 65
    • 0026108980 scopus 로고
    • Free Energy and Temperature Dependence of Electron Transfer at the Metal-Electrolyte Interface
    • Chidsey, C. E. D. Free Energy and Temperature Dependence of Electron Transfer at the Metal-Electrolyte Interface Science 1991, 251, 919-922
    • (1991) Science , vol.251 , pp. 919-922
    • Chidsey, C.E.D.1
  • 66
    • 49249148639 scopus 로고
    • General Expression of the Linear Potential Sweep Voltammogram in the Case of Diffusionless Electrochemical Systems
    • Laviron, E. General Expression of the Linear Potential Sweep Voltammogram in the Case of Diffusionless Electrochemical Systems J. Electroanal. Chem. 1979, 101, 19-28
    • (1979) J. Electroanal. Chem. , vol.101 , pp. 19-28
    • Laviron, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.