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Volumn 118, Issue 30, 2014, Pages 16710-16717

Engineering a robust photovoltaic device with quantum dots and bacteriorhodopsin

(13)  Renugopalakrishnan, Venkatesan a,b   Barbiellini, Bernardo b   King, Chris b   Molinari, Michael c   Mochalov, Konstantin d   Sukhanova, Alyona c,d   Nabiev, Igor c,d   Fojan, Peter e   Tuller, Harry L f   Chin, Michael g   Somasundaran, Ponisseril g   Padrós, Esteve h   Ramakrishna, Seeram i  


Author keywords

[No Author keywords available]

Indexed keywords

DEPOSITION; DYE-SENSITIZED SOLAR CELLS; ENERGY TRANSFER; GOLD; HYBRID MATERIALS; SEMICONDUCTOR QUANTUM DOTS; SOLAR CELLS;

EID: 84905457640     PISSN: 19327447     EISSN: 19327455     Source Type: Journal    
DOI: 10.1021/jp502885s     Document Type: Article
Times cited : (52)

References (50)
  • 1
    • 0035891138 scopus 로고    scopus 로고
    • Photoelectrochemical Cells
    • Gratzel, M. Photoelectrochemical Cells Nature 2001, 414, 338-344
    • (2001) Nature , vol.414 , pp. 338-344
    • Gratzel, M.1
  • 2
    • 0037421918 scopus 로고    scopus 로고
    • Applied Physics: Solar Cells to Dye for
    • Gratzel, M. Applied Physics: Solar Cells to Dye For Nature 2003, 421, 586-587
    • (2003) Nature , vol.421 , pp. 586-587
    • Gratzel, M.1
  • 3
    • 58549109182 scopus 로고    scopus 로고
    • Controlled Electron Injection and Transport at Materials Interfaces in Dye Sensitized Solar Cells
    • Thavasi, V.; Renugopalakrishnan, V.; Jose, R.; Ramakrishna, S. Controlled Electron Injection and Transport at Materials Interfaces in Dye Sensitized Solar Cells Mater. Sci. Eng., R 2009, 63, 81-99
    • (2009) Mater. Sci. Eng., R , vol.63 , pp. 81-99
    • Thavasi, V.1    Renugopalakrishnan, V.2    Jose, R.3    Ramakrishna, S.4
  • 4
    • 0037421863 scopus 로고    scopus 로고
    • A Photovoltaic Device Structure Based on Internal Electron Emission
    • McFarland, E. W.; Tang, J. A Photovoltaic Device Structure Based on Internal Electron Emission Nature 2003, 421, 616-618
    • (2003) Nature , vol.421 , pp. 616-618
    • McFarland, E.W.1    Tang, J.2
  • 7
    • 84855835025 scopus 로고    scopus 로고
    • A Transporter Converted into a Sensor, a Phototaxis Signaling Mutant of Bacteriorhodopsin at 3.0 A
    • Spudich, E. N.; Ozorowski, G.; Schow, E. V.; Tobias, D. J.; Spudich, J. L.; Luecke, H. A Transporter Converted Into a Sensor, a Phototaxis Signaling Mutant of Bacteriorhodopsin at 3.0 A Mol. Biol. 2012, 415, 455-463
    • (2012) Mol. Biol. , vol.415 , pp. 455-463
    • Spudich, E.N.1    Ozorowski, G.2    Schow, E.V.3    Tobias, D.J.4    Spudich, J.L.5    Luecke, H.6
  • 9
    • 0028864699 scopus 로고
    • Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin
    • Brown, L. S.; Sasaki, J.; Kandori, H.; Maeda, A.; Needleman, R.; Lanyi, J. K. Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin J. Biol. Chem. 1995, 270, 27122-27126
    • (1995) J. Biol. Chem. , vol.270 , pp. 27122-27126
    • Brown, L.S.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 10
    • 0001086464 scopus 로고    scopus 로고
    • Ballistic Electron Transport Through Au(111)/Si(111) and Au(111)/Si(100) Interfaces
    • Weilmeier, M. K.; Rippard, W. H.; Buhrman, R. A. Ballistic Electron Transport Through Au(111)/Si(111) and Au(111)/Si(100) Interfaces Phys. Rev. B 1999, 59, R2521-R2524
    • (1999) Phys. Rev. B , vol.59
    • Weilmeier, M.K.1    Rippard, W.H.2    Buhrman, R.A.3
  • 14
    • 84872691479 scopus 로고    scopus 로고
    • Basic Principles and Current Trends in Colloidal Synthesis of Highly Luminescent Semiconductor Nanocrystals
    • Samokhvalov, P.; Artemyev, M.; Nabiev, I. Basic Principles and Current Trends in Colloidal Synthesis of Highly Luminescent Semiconductor Nanocrystals Chem.-Eur. J. 2013, 19, 1534-1546
    • (2013) Chem.-Eur. J. , vol.19 , pp. 1534-1546
    • Samokhvalov, P.1    Artemyev, M.2    Nabiev, I.3
  • 15
    • 36549026305 scopus 로고    scopus 로고
    • Stationary Current Generated from Photocycle of a Hybrid Bacteriorhodopsin/quantum Dot Bionanosystem
    • Li, R.; Li, C. M.; Bao, H.; Bao, Q.; Lee, V. S. Stationary Current Generated from Photocycle of a Hybrid Bacteriorhodopsin/quantum Dot Bionanosystem Appl. Phys. Lett. 2007, 91, 223901-223901-3
    • (2007) Appl. Phys. Lett. , vol.91 , pp. 223901-2239013
    • Li, R.1    Li, C.M.2    Bao, H.3    Bao, Q.4    Lee, V.S.5
  • 16
    • 77955341350 scopus 로고    scopus 로고
    • Resonance Energy Transfer Improves the Biological Function of Bacteriorhodopsin Within a Hybrid Material Built from Purple Membranes and Semiconductor Quantum Dots
    • Rakovich, A.; Sukhanova, A.; Bouchonville, N.; Lukashev, E.; Oleinikov, V.; Artemyev, M.; Lesnyak, V.; Gaponik, N.; Molinari, M.; Troyon, M. Resonance Energy Transfer Improves the Biological Function of Bacteriorhodopsin Within a Hybrid Material Built from Purple Membranes and Semiconductor Quantum Dots Nano Lett. 2010, 10, 2640-2648
    • (2010) Nano Lett. , vol.10 , pp. 2640-2648
    • Rakovich, A.1    Sukhanova, A.2    Bouchonville, N.3    Lukashev, E.4    Oleinikov, V.5    Artemyev, M.6    Lesnyak, V.7    Gaponik, N.8    Molinari, M.9    Troyon, M.10
  • 17
    • 78651297470 scopus 로고    scopus 로고
    • Charge-Controlled Assembling of Bacteriorhodopsin and Semiconductor Quantum Dots for Fluorescence Resonance Energy Transfer-Based Nanophotonic Applications
    • Bouchonville, N.; Molinari, M.; Sukhanova, A.; Artemyev, M.; Oleinikov, V. A.; Troyon, M.; Nabiev, I. Charge-Controlled Assembling of Bacteriorhodopsin and Semiconductor Quantum Dots for Fluorescence Resonance Energy Transfer-Based Nanophotonic Applications. Appl. Phys. Lett. 2011, 98, 013703.
    • (2011) Appl. Phys. Lett. , vol.98 , pp. 013703
    • Bouchonville, N.1    Molinari, M.2    Sukhanova, A.3    Artemyev, M.4    Oleinikov, V.A.5    Troyon, M.6    Nabiev, I.7
  • 18
    • 84881295653 scopus 로고    scopus 로고
    • Nano-Biophotonic Hybrid Materials with Controlled FRET Efficiency Engineered from Quantum Dots and Bacteriorhodopsin
    • Bouchonville, N.; Cigne, A. L.; Sukhanova, A.; Molinari, M.; Nabiev, I. Nano-Biophotonic Hybrid Materials with Controlled FRET Efficiency Engineered from Quantum Dots and Bacteriorhodopsin Laser Phys. Lett. 2013, 10, 085901
    • (2013) Laser Phys. Lett. , vol.10 , pp. 085901
    • Bouchonville, N.1    Cigne, A.L.2    Sukhanova, A.3    Molinari, M.4    Nabiev, I.5
  • 19
    • 84858057879 scopus 로고    scopus 로고
    • Exactly Soluble Model of Resonant Energy Transfer between Molecules
    • King, C.; Barbiellini, B.; Moser, D.; Renugopalakrishnan, V. Exactly Soluble Model of Resonant Energy Transfer Between Molecules Phys. Rev. B 2012, 85, 125106
    • (2012) Phys. Rev. B , vol.85 , pp. 125106
    • King, C.1    Barbiellini, B.2    Moser, D.3    Renugopalakrishnan, V.4
  • 20
    • 33646370530 scopus 로고    scopus 로고
    • The Healing Mechanism for Excited Molecules Near Metallic Surfaces
    • Barbiellini, B.; Platzman, P. M. The Healing Mechanism for Excited Molecules Near Metallic Surfaces New J. Phys. 2006, 8, 20
    • (2006) New J. Phys. , vol.8 , pp. 20
    • Barbiellini, B.1    Platzman, P.M.2
  • 21
    • 77953727847 scopus 로고    scopus 로고
    • Auger-Mediated Sticking of Positrons to Surfaces: Evidence for a Single-Step Transition from a Scattering State to a Surface Image Potential Bound State
    • Mukherjee, S.; Nadesalingam, M. P.; Guagliardo, P.; Sergeant, A. D.; Barbiellini, B.; Williams, J. F.; Fazleev, N. G.; Weiss, A. H. Auger-Mediated Sticking of Positrons to Surfaces: Evidence for a Single-Step Transition from a Scattering State to a Surface Image Potential Bound State Phys. Rev. Lett. 2010, 104, 247403
    • (2010) Phys. Rev. Lett. , vol.104 , pp. 247403
    • Mukherjee, S.1    Nadesalingam, M.P.2    Guagliardo, P.3    Sergeant, A.D.4    Barbiellini, B.5    Williams, J.F.6    Fazleev, N.G.7    Weiss, A.H.8
  • 25
    • 13644249781 scopus 로고    scopus 로고
    • Deactivation of Au/CeOx Water Gas Shift Catalysts
    • Kim, C. H.; Thompson, L. T. Deactivation of Au/CeOx Water Gas Shift Catalysts J. Catal. 2005, 230, 66-74
    • (2005) J. Catal. , vol.230 , pp. 66-74
    • Kim, C.H.1    Thompson, L.T.2
  • 26
    • 77949962141 scopus 로고    scopus 로고
    • Theory and Simulation of Nanostructured Materials for Photovoltaic Applications
    • Kanai, Y.; Neaton, J. B.; Grossman, J. C. Theory and Simulation of Nanostructured Materials for Photovoltaic Applications Comput. Sci. Eng. 2010, 12, 18-27
    • (2010) Comput. Sci. Eng. , vol.12 , pp. 18-27
    • Kanai, Y.1    Neaton, J.B.2    Grossman, J.C.3
  • 27
    • 0000361423 scopus 로고    scopus 로고
    • Stochastic Gradient Approximation: An Efficient Method to Optimize Many-Body Wave Functions
    • Harju, A.; Barbiellini, B.; Siljamäki, S.; Nieminen, R. M.; Ortiz, G. Stochastic Gradient Approximation: An Efficient Method to Optimize Many-Body Wave Functions Phys. Rev. Lett. 1997, 79, 1173-1177
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 1173-1177
    • Harju, A.1    Barbiellini, B.2    Siljamäki, S.3    Nieminen, R.M.4    Ortiz, G.5
  • 28
    • 84905501746 scopus 로고    scopus 로고
    • Spectroscopic Determination of HOMO and LUMO Energies of Retinal in Bacteriorhodopsin for Solar Cell Applications
    • Xingyu, G.; Viswanathan, S. N.; Chang, C.-W.; Barbiellini, B.; Budil, D. E.; Renugopalakrishnan, V. Spectroscopic Determination of HOMO and LUMO Energies of Retinal in Bacteriorhodopsin for Solar Cell Applications Biophys. J. 2010, 98, 172
    • (2010) Biophys. J. , vol.98 , pp. 172
    • Xingyu, G.1    Viswanathan, S.N.2    Chang, C.-W.3    Barbiellini, B.4    Budil, D.E.5    Renugopalakrishnan, V.6
  • 33
    • 84866356273 scopus 로고    scopus 로고
    • Thin Films and Assemblies of Photosensitive Membrane Proteins and Colloidal Nanocrystals for Engineering of Hybrid Materials with Advanced Properties
    • Zaitsev, S. Y.; Solovyeva, D. O.; Nabiev, I. Thin Films and Assemblies of Photosensitive Membrane Proteins and Colloidal Nanocrystals for Engineering of Hybrid Materials with Advanced Properties Adv. Colloid Interface Sci. 2012, 183-184, 14-29
    • (2012) Adv. Colloid Interface Sci. , vol.183-184 , pp. 14-29
    • Zaitsev, S.Y.1    Solovyeva, D.O.2    Nabiev, I.3
  • 34
    • 0032770157 scopus 로고    scopus 로고
    • Opening the Schiff Base Moiety of Bacteriorhodopsin by Mutation of the Four Extracellular Glu Side Chains
    • Sanz, C.; Lazarova, T.; Sepulcre, F.; Gonz‡lez-Moreno, R.; Bourdelande, J. L.; Querol, E.; Padrós, E. Opening the Schiff Base Moiety of Bacteriorhodopsin by Mutation of the Four Extracellular Glu Side Chains FEBS Lett. 1999, 456, 191-195
    • (1999) FEBS Lett. , vol.456 , pp. 191-195
    • Sanz, C.1    Lazarova, T.2    Sepulcre, F.3    Gonzlez-Moreno, R.4    Bourdelande, J.L.5    Querol, E.6    Padrós, E.7
  • 35
    • 0027536538 scopus 로고
    • Homologous Bacterio-Opsin-Encoding Gene Expression via Site-Specific Vector Integration
    • Ferrando, E.; Schweiger, U.; Oesterhelt, D. Homologous Bacterio-Opsin-Encoding Gene Expression via Site-Specific Vector Integration Gene 1993, 125, 41-47
    • (1993) Gene , vol.125 , pp. 41-47
    • Ferrando, E.1    Schweiger, U.2    Oesterhelt, D.3
  • 36
    • 0016376428 scopus 로고
    • Isolation of the Cell Membrane of Halobacterium Halobium and Its Fractionation into Red and Purple Membrane
    • Oesterhelt, D.; Stoeckenius, W. Isolation of the Cell Membrane of Halobacterium Halobium and Its Fractionation Into Red and Purple Membrane Methods Enzymol. 1974, 31, 667-678
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 37
    • 0001648770 scopus 로고    scopus 로고
    • Resolution and Contrast in Kelvin Probe Force Microscopy
    • Jacobs, H. O.; Leuchtmann, P.; Homan, O. J.; Stemmer, A. Resolution and Contrast in Kelvin Probe Force Microscopy J. Appl. Phys. 1998, 84, 1168-1173
    • (1998) J. Appl. Phys. , vol.84 , pp. 1168-1173
    • Jacobs, H.O.1    Leuchtmann, P.2    Homan, O.J.3    Stemmer, A.4
  • 38
    • 33745478167 scopus 로고    scopus 로고
    • Photoinduced Surface Potential Change of Bacteriorhodopsin Mutant D96N Measured by Scanning Surface Potential Microscopy
    • Lee, I.; Greenbaum, E.; Budy, S.; Hillebrecht, J. R.; Birge, R. R.; Stuart, J. Photoinduced Surface Potential Change of Bacteriorhodopsin Mutant D96N Measured by Scanning Surface Potential Microscopy J. Phys. Chem. B 2006, 110, 10982-10990
    • (2006) J. Phys. Chem. B , vol.110 , pp. 10982-10990
    • Lee, I.1    Greenbaum, E.2    Budy, S.3    Hillebrecht, J.R.4    Birge, R.R.5    Stuart, J.6
  • 39
    • 0036472252 scopus 로고    scopus 로고
    • Imaging the Surface Potential of Active Purple Membrane
    • Knapp, H. F.; Mesquida, P.; Stemmer, A. Imaging the Surface Potential of Active Purple Membrane Surf. Interface Anal. 2002, 33, 108-112
    • (2002) Surf. Interface Anal. , vol.33 , pp. 108-112
    • Knapp, H.F.1    Mesquida, P.2    Stemmer, A.3
  • 41
    • 0031750973 scopus 로고    scopus 로고
    • Conformational Changes: How Small Is Big Enough?
    • Koshland, D. Conformational Changes: How Small Is Big Enough? Nat. Med. 1998, 4, 1112-1114
    • (1998) Nat. Med. , vol.4 , pp. 1112-1114
    • Koshland, D.1
  • 42
    • 48749126860 scopus 로고    scopus 로고
    • Insights into Protein Flexibility: The Relationship between Normal Modes and Conformational Change Upon Protein-Protein Docking
    • Dobbins, S. E.; Lesk, V.; Sternberg, M. J. E. Insights Into Protein Flexibility: The Relationship Between Normal Modes and Conformational Change Upon Protein-Protein Docking Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 10390-10395
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10390-10395
    • Dobbins, S.E.1    Lesk, V.2    Sternberg, M.J.E.3
  • 43
    • 0025947168 scopus 로고
    • Mechanism of Proton Pumping in Bacteriorhodopsin by Solid-State NMR: The Protonation State of Tyrosine in the Light-Adapted and M States
    • McDermott, A. E.; Thompson, L. K.; Winkel, C.; Farrar, M. R.; Pelletier, S.; Lugtenburg, J.; Herzfeld, J.; Griffin, R. G. Mechanism of Proton Pumping in Bacteriorhodopsin by Solid-State NMR: The Protonation State of Tyrosine in the Light-Adapted and M States Biochemistry 1991, 30, 8366-8371
    • (1991) Biochemistry , vol.30 , pp. 8366-8371
    • McDermott, A.E.1    Thompson, L.K.2    Winkel, C.3    Farrar, M.R.4    Pelletier, S.5    Lugtenburg, J.6    Herzfeld, J.7    Griffin, R.G.8
  • 44
    • 0029026347 scopus 로고
    • Structure and Fluctuations of Bacteriorhodopsin in the Purple Membrane: A Molecular Dynamics Study
    • Edholm, O.; Berger, O.; Jähnig, F. Structure and Fluctuations of Bacteriorhodopsin in the Purple Membrane: A Molecular Dynamics Study J. Mol. Biol. 1995, 250, 94-111
    • (1995) J. Mol. Biol. , vol.250 , pp. 94-111
    • Edholm, O.1    Berger, O.2    Jähnig, F.3
  • 45
    • 0020688832 scopus 로고
    • Calculation of Volume Fluctuation for Globular Protein Models
    • Lee, B. Calculation of Volume Fluctuation for Globular Protein Models Proc. Natl. Acad. Sci. U. S. A. 1983, 80, 622-626
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 622-626
    • Lee, B.1
  • 46
    • 0000411306 scopus 로고    scopus 로고
    • Constant-Pressure Molecular Dynamics Techniques Applied to Complex Molecular Systems and Solvated Proteins
    • Paci, E.; Marchi, M. Constant-Pressure Molecular Dynamics Techniques Applied to Complex Molecular Systems and Solvated Proteins J. Phys. Chem. 1996, 100, 4314-4322
    • (1996) J. Phys. Chem. , vol.100 , pp. 4314-4322
    • Paci, E.1    Marchi, M.2
  • 47
    • 6444224645 scopus 로고
    • Flexibility of Enzymes Suspended in Organic Solvents Probed by Time-Resolved Fluorescence Anisotropy. Evidence That Enzyme Activity and Enantioselectivity Are Directly Related to Enzyme Flexibility
    • Broos, J.; Visser, A. J. W. G.; Engbersen, J. F. J.; Verboom, W.; van Hoek, A.; Reinhoudt, D. N. Flexibility of Enzymes Suspended in Organic Solvents Probed by Time-Resolved Fluorescence Anisotropy. Evidence That Enzyme Activity and Enantioselectivity Are Directly Related to Enzyme Flexibility J. Am. Chem. Soc. 1995, 117, 12657-12663
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12657-12663
    • Broos, J.1    Visser, A.J.W.G.2    Engbersen, J.F.J.3    Verboom, W.4    Van Hoek, A.5    Reinhoudt, D.N.6
  • 49
    • 4143127620 scopus 로고    scopus 로고
    • Hydration of Enzyme in Nonaqueous Media Is Consistent with Solvent Dependence of Its Activity
    • Yang, L.; Dordick, J. S.; Garde, S. Hydration of Enzyme in Nonaqueous Media Is Consistent with Solvent Dependence of Its Activity Biophys. J. 2004, 87, 812-821
    • (2004) Biophys. J. , vol.87 , pp. 812-821
    • Yang, L.1    Dordick, J.S.2    Garde, S.3
  • 50
    • 84896399759 scopus 로고    scopus 로고
    • Enzyme Activity and Structural Dynamics Linked to Micelle Formation: A Fluorescence Anisotropy and ESR Study
    • Chin, M.; Somasundaran, P. Enzyme Activity and Structural Dynamics Linked to Micelle Formation: A Fluorescence Anisotropy and ESR Study Photochem. Photobiol. 2014, 90, 455-462.
    • (2014) Photochem. Photobiol. , vol.90 , pp. 455-462
    • Chin, M.1    Somasundaran, P.2


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