Structural and Functional Hierarchy in Photosynthetic Energy Conversion—from Molecules to Nanostructures (original) (raw)
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Bio-inspired photo-electronic material based on photosynthetic proteins
2009
The construction of efficient light energy converting (photovoltaic and photo-electronic) devices is a current and great challenge in science and technology and one that will have important economic consequences. Several innovative nanoelectronic materials were proposed to achieve this goal, semiconductor quantum dots, metallic nanowires and carbon nanotubes (CNT) are among them. As a charge separating unit for light energy conversion, we propose the utilization of the most advanced photoelectronic material developed by nature, photosynthetic reaction center proteins. As a first step in this direction, we constructed a novel bioinorganic nanophotoelectronic material with photoactive photosynthetic reaction center (RC) proteins encapsulated inside a multiwall CNT arrayed electrode. The material consists of photosynthetic RC-cytochrome complexes acting as charge separating units bound to the inner walls of a CNT electrode and ubiquinone-10 (Q2) serving as a soluble electron-transfer mediator to the counter electrode. The proteins were immobilized inside carbon nanotubes by a Ni(NTA)-alkane-pyrene linker, forming a self-assembled monolayer (SAM) on the surface of inner CNT walls and allowing for unidirectional protein orientation. The material demonstrates an enhanced photoinduced electron transfer rate and shows substantial improvement in photocurrent density compared to that obtained with the same proteins when immobilized on planar graphite (HOPG) electrode. The results suggest that protein encapsulation in precisely organized arrayed tubular electrode architecture can considerably improve the performance of photovoltaic, photoelectronic, or biofuel cell devices. They demonstrate the potential for substantial advantages of precisely organized nano electrode tubular arrayed architecture for variety biotechnological applications.
Photosynthetic reaction center protein in nanostructures
… status solidi (b), 2011
Photosynthetic reaction center (RC) is one of the most important proteins, because it is Nature's solar battery converting light energy into chemical potential in the photosynthetic membrane assuring conditions for carbon reduction in cells. Although it is developed in nanometer scale, and is working in nanoscopic power, this is the protein that assures the energy input practically for the whole biosphere on Earth. The extremely large quantum yield of the primary charge separation (close to 100%) in the RC offers a big challenge to use it in nanodevices. Results of structural (AFM, EM), optical, and electro chemical investigations on RC bio-nanocomposite materials based on different carrier matrices (e.g., CNTs, ITO) will be presented.
Bio-inspired photo-electronic material based on photosynthetic proteins
Nanobiosystems: Processing, Characterization, and Applications II, 2009
The construction of efficient light energy converting (photovoltaic and photo-electronic) devices is a current and great challenge in science and technology and one that will have important economic consequences. Several innovative nanoelectronic materials were proposed to achieve this goal, semiconductor quantum dots, metallic nanowires and carbon nanotubes (CNT) are among them. As a charge separating unit for light energy conversion, we propose the utilization of the most advanced photoelectronic material developed by nature, photosynthetic reaction center proteins. As a first step in this direction, we constructed a novel bioinorganic nanophotoelectronic material with photoactive photosynthetic reaction center (RC) proteins encapsulated inside a multiwall CNT arrayed electrode. The material consists of photosynthetic RC-cytochrome complexes acting as charge separating units bound to the inner walls of a CNT electrode and ubiquinone-10 (Q2) serving as a soluble electron-transfer mediator to the counter electrode. The proteins were immobilized inside carbon nanotubes by a Ni(NTA)-alkanepyrene linker, forming a self-assembled monolayer (SAM) on the surface of inner CNT walls and allowing for unidirectional protein orientation. The material demonstrates an enhanced photoinduced electron transfer rate and shows substantial improvement in photocurrent density compared to that obtained with the same proteins when immobilized on planar graphite (HOPG) electrode. The results suggest that protein encapsulation in precisely organized arrayed tubular electrode architecture can considerably improve the performance of photovoltaic, photoelectronic, or biofuel cell devices. They demonstrate the potential for substantial advantages of precisely organized nano electrode tubular arrayed architecture for variety biotechnological applications.
Nanosized Optoelectronic Devices Based on Photoactivated Proteins
Biomacromolecules, 2012
Molecular nanoelectronics is attracting much attention, because of the possibility to add functionalities to silicon-based electronics by means of intrinsically nanoscale biological or organic materials. The contact point between active molecules and electrodes must present, besides nanoscale size, a very low resistance. To realize Metal-Molecule-Metal junctions it is, thus, mandatory to be able to control the formation of useful nanometric contacts. The distance between the electrodes has to be of the same size of the molecule being put in between. Nanogaps technology is a perfect fit to fulfill this requirement. In this work, nanogaps between gold electrodes have been used to develop optoelectronic devices based on photoactive proteins. Reaction Centers (RC) and Bacteriorhodopsin (BR) have been inserted in nanogaps by drop casting. Electrical characterizations of the obtained structures were performed. It has been demonstrated that these nanodevices working principle is based on charge separation and photovoltage response. The former is induced by the application of a proper voltage on the RC, while the latter comes from the activation of BR by light of appropriate wavelengths.
Biomacromolecules, 2014
Photosynthetic compounds have been a paradigm for biosolar cells and biosensors and for application in photovoltaic and photocatalytic devices. However, the interconnection of proteins and protein complexes with electrodes, in terms of electronic contact, structure, alignment and orientation, remains a challenge. Here we report on a deposition method that relies on the self-organizing properties of these biological protein complexes to produce a densely packed monolayer by using Langmuir-Blodgett technology. The monolayer is deposited onto a gold electrode with defined orientation and produces the highest light-induced photocurrents per protein complex to date, 45 μA/cm(2) (with illumination power of 23 mW/cm(2) at 880 nm), under ambient conditions. Our work shows for the first time that a significant portion of the intrinsic quantum efficiency of primary photosynthesis can be retained outside the biological cell, leading to an internal quantum efficiency (absorbed photon to electro...
Advanced Materials, 2005
Photosystem I (PS I) is a transmembrane, multi-subunit protein-chlorophyll complex that mediates vectorial, light-induced electron transfer. The nanometer-sized dimensions, an energy yield of approximately 58 %, and the quantum effi-ciency of almost 1 make the reaction center a promising unit for applications in molecular nanoelectronics. PS I is located in the thylakoid membranes of chloroplasts and cyanobacteria. It mediates light-induced electron transfer from plastocyanin or cytochrome C 553 to ferredoxin. The crystalline structure of PS I from Synechococus elongatus and from plants' chloroplast was resolved to 2.5 and 4.4 Å, respectively. In cyanobacteria, the complex consists of at least 12 polypeptides, some of which bind 96 light-harvesting chlorophyll molecules. The electron-transport chain contains P700, A 0 , A 1 , F X , F A , and F B , representing a chlorophyll a dimer, a monomeric chlorophyll a, two phylloquinones, and three [4Fe-4S] iron-sulfur centers, respectively. The reaction-center core complex is made up of the heterodimeric PsaA and PsaB subunits, containing the primary electron donor, P700, which undergoes light-induced charge separation and transfers an electron through the sequential carriers A 0 , A 1 , and F X . The final acceptors, F A and F B , are located on another subunit, PsaC. The redox potential of the primary donor, P700, is +0.43 V and that of the final acceptor, F B , is -0.53 V, producing a redox difference of -1.0 V. The charge separation spans about 5 nm of the height of the protein, representing the center-tocenter distance between the primary donor and the final acceptor. The protein complex is 9 nm in height and has a diameter of 21 nm and 15 nm for the trimer and the monomer, respectively. The photoactivity and the nanometer-sized dimensions make this complex a promising unit for applications in molecular nanoelectronics. In earlier works, care was taken to indirectly attach plant PS I and bacterial reaction centers to solid surfaces in attempts avoid inactivation of selfassembled monolayers.
Photosynthetic reaction centers/ITO hybrid nanostructure
Materials Science and Engineering: C, 2013
Photosynthetic reaction center proteins purified from Rhodobacter sphaeroides purple bacterium were deposited on the surface of indium tin oxide (ITO), a transparent conductive oxide, and the photochemical/-physical properties of the composite were investigated. The kinetics of the light induced absorption change indicated that the RC was active in the composite and there was an interaction between the protein cofactors and the ITO. The electrochromic response of the bacteriopheophytine absorption at 771 nm showed an increased electric field perturbation around this chromophore on the surface of ITO compared to the one measured in solution. This absorption change is associated with the chargecompensating relaxation events inside the protein. Similar life time, but smaller magnitude of this absorption change was measured on the surface of borosilicate glass. The light induced change in the conductivity of the composite as a function of the concentration showed the typical sigmoid saturation characteristics unlike if the photochemically inactive chlorophyll was layered on the ITO. In this later case the light induced change in the conductivity was oppositely proportional to the chlorophyll concentration due to the thermal dissipation of the excitation energy. The sensitivity of the measurement is very high, few picomole RC can change the light induced resistance of the composite.
Biomacromolecules, 2012
A polyhistidine (His) tag was fused to the C-or Nterminus of the light-harvesting (LH1)-α chain of the photosynthetic antenna core complex (LH1-RC) from Rhodobacter sphaeroides to allow immobilization of the complex on a solid substrate with defined orientation. His-tagged LH1-RCs were adsorbed onto a gold electrode modified with Ni-NTA. The LH1-RC with the C-terminal His-tag (C-His LH1-RC) on the modified electrode produced a photovoltaic response upon illumination. Electron transfer is unidirectional within the RC and starts when the bacteriochlorophyll a dimer in the RC is activated by light absorbed by LH1. The LH1-RC with the Nterminal His-tag (N-His LH1-RC) produced very little or no photocurrent upon illumination at any wavelength. The conductivity of the His-tagged LH1-RC was measured with point-contact current imaging atomic force microscopy, indicating that 60% of the C-His LH1-RC are correctly oriented (N-His 63%). The oriented C-His LH1-RC or N-His LH1-RC showed semiconductive behavior, that is, had the opposite orientation. These results indicate that the His-tag successfully controlled the orientation of the RC on the solid substrate, and that the RC produced photocurrent depending upon the orientation on the electrode.