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1.
Bioelectrochemistry ; 146: 108138, 2022 Aug.
Article in English | MEDLINE | ID: mdl-35487144

ABSTRACT

In order to elucidate the old, still unsolved problem of how the diffuse electric double layer responds to an abrupt, intramolecular charge displacement inside a biological membrane, we investigated the fastest components of the light-induced electric signals of bacteriorhodopsin and its mutants, in numerous ionic and buffer solutions. The obtained data for temperature and solute concentration dependence were interpreted as a consequence of changes in the capacity of the diffuse double layer surrounding the purple membrane. The possible physiological consequences of this so far not demonstrated phenomenon are discussed.


Subject(s)
Bacteriorhodopsins , Light , Bacteriorhodopsins/physiology , Cell Membrane , Electricity , Temperature
2.
Biochemistry (Mosc) ; 85(Suppl 1): S196-S212, 2020 Jan.
Article in English | MEDLINE | ID: mdl-32087060

ABSTRACT

Rhodopsins are light-sensitive membrane proteins enabling transmembrane charge separation (proton pump) on absorption of a light quantum. Bacteriorhodopsin (BR) is a transmembrane protein from halophilic bacteria that belongs to the rhodopsin family. Potential applications of BR are considered so promising that the number of studies devoted to the use of BR itself, its mutant variants, as well as hybrid materials containing BR in various areas grows steadily. Formation of hybrid structures combining BR with nanoparticles is an essential step in promotion of BR-based devices. However, rapid progress, continuous emergence of new data, as well as challenges of analyzing the entire data require regular reviews of the achievements in this area. This review is devoted to the issues of formation of materials based on hybrids of BR with fluorescent semiconductor nanocrystals (quantum dots) and with noble metal (silver, gold) plasmonic nanoparticles. Recent data on formation of thin (mono-) and thick (multi-) layers from materials containing BR and BR/nanoparticle hybrids are presented.


Subject(s)
Bacteriorhodopsins/chemistry , Bacteriorhodopsins/physiology , Metal Nanoparticles/chemistry , Quantum Dots/chemistry , Electromagnetic Fields , Gold/chemistry , Gold/metabolism , Halobacterium salinarum/cytology , Purple Membrane/metabolism , Retinal Rod Photoreceptor Cells/metabolism , Rhodopsin/chemistry , Semiconductors , Silver/chemistry , Silver/metabolism , Spectrum Analysis, Raman
3.
ACS Appl Mater Interfaces ; 6(4): 2799-808, 2014 Feb 26.
Article in English | MEDLINE | ID: mdl-24498928

ABSTRACT

The Q photoproduct of bacteriorhodopsin (BR) is the basis of several biophotonic technologies that employ BR as the photoactive element. Several blue BR (bBR) mutants, generated by using directed evolution, were investigated with respect to the photochemical formation of the Q state. We report here a new bBR mutant, D85E/D96Q, which is capable of efficiently converting the entire sample to and from the Q photoproduct. At pH 8.5, where Q formation is optimal, the Q photoproduct requires 65 kJ mol(-1) of amber light irradiation (590 nm) for formation and 5 kJ mol(-1) of blue light (450 nm) for reversion, respectively. The melting temperature of the resting state and Q photoproduct, measured via differential scanning calorimetry, is observed at 100 °C and 89 °C at pH 8.5 or 91 °C and 82 °C at pH 9.5, respectively. We hypothesize that the protein stability of D85E/D96Q compared to other blue mutants is associated with a rapid equilibrium between the blue form E85(H) and the purple form E85(-) of the protein, the latter providing enhanced structural stability. Additionally, the protein is shown to be stable and functional when suspended in an acrylamide matrix at alkaline pH. Real-time photoconversion to and from the Q state is also demonstrated with the immobilized protein. Finally, the holographic efficiency of an ideal thin film using the Q state of D85E/D96Q is calculated to be 16.7%, which is significantly better than that provided by native BR (6-8%) and presents the highest efficiency of any BR mutant to date.


Subject(s)
Bacteriorhodopsins/physiology , Bacteriorhodopsins/chemistry , Bacteriorhodopsins/genetics , Calorimetry, Differential Scanning , Hot Temperature , Hydrogen-Ion Concentration , Spectrophotometry, Ultraviolet
4.
Nanotechnology ; 24(39): 395501, 2013 Oct 04.
Article in English | MEDLINE | ID: mdl-24013479

ABSTRACT

The increasing interest in photoactivated proteins as natural replacements for standard inorganic materials in photocells leads to the comparison analysis of bacteriorhodopsin and proteorhodopsin, two widely diffused proteins belonging to the family of type-1 opsins. These proteins share similar behaviors but exhibit relevant differences in the sequential chain of the amino acids constituting their tertiary structure. The use of an impedance network analog to model the protein main features provides a microscopic interpretation of a set of experiments on their photo-conductance properties. In particular, this model links the protein electrical responses to the tertiary structure and to the interactions between neighboring amino acids. The same model is also used to predict the small-signal response in terms of the Nyquist plot. Interestingly, these rhodopsins are found to behave like a wide-gap semiconductor with intrinsic conductivities of the order of 10⁻7 S cm⁻¹.


Subject(s)
Bacteriorhodopsins , Rhodopsin , Bacteriorhodopsins/chemistry , Bacteriorhodopsins/physiology , Computer Simulation , Electric Impedance , Models, Biological , Rhodopsin/chemistry , Rhodopsin/physiology , Rhodopsins, Microbial
5.
Phys Rev E Stat Nonlin Soft Matter Phys ; 81(3 Pt 1): 032902, 2010 Mar.
Article in English | MEDLINE | ID: mdl-20365799

ABSTRACT

We report on electrical properties of the two sensing proteins: bacteriorhodopsin and rat olfactory receptor OR-I7. As relevant transport parameters we consider the small-signal impedance spectrum and the static current-voltage characteristics. Calculations are compared with available experimental results and the model predictability is tested for future perspectives.


Subject(s)
Bacteriorhodopsins/chemistry , Bacteriorhodopsins/physiology , Models, Biological , Models, Chemical , Receptors, Odorant/chemistry , Receptors, Odorant/physiology , Animals , Bacteriorhodopsins/ultrastructure , Computer Simulation , Electric Conductivity , Rats , Receptors, Odorant/ultrastructure
6.
Math Biosci ; 225(1): 68-80, 2010 May.
Article in English | MEDLINE | ID: mdl-20188746

ABSTRACT

The archaeon Halobacterium salinarum can grow phototrophically with only light as its energy source. It uses the retinal containing and light-driven proton pump bacteriorhodopsin to enhance the membrane potential which drives the ATP synthase. Therefore, a model of the membrane potential generation of bacteriorhodopsin is of central importance to the development of a mathematical model of the bioenergetics of H. salinarum. To measure the current produced by bacteriorhodopsin at different light intensities and clamped voltages, we expressed the gene in Xenopus laevis oocytes. We present current-voltage measurements and a mathematical model of the current-voltage relationship of bacteriorhodopsin and its generation of the membrane potential. The model consists of three intermediate states, the BR, L, and M states, and comparisons between model predictions and experimental data show that the L to M reaction must be inhibited by the membrane potential. The model is not able to fit the current-voltage measurements when only the M to BR phase is membrane potential dependent, while it is able to do so when either only the L to M reaction or both reactions (L to M and M to BR) are membrane potential dependent. We also show that a decay term is necessary for modeling the rate of change of the membrane potential.


Subject(s)
Bacteriorhodopsins/physiology , Halobacterium salinarum/physiology , Membrane Potentials/physiology , Models, Biological , Animals , Bacteriorhodopsins/genetics , Female , Patch-Clamp Techniques , Transfection , Xenopus laevis
7.
Photochem Photobiol ; 86(2): 316-23, 2010.
Article in English | MEDLINE | ID: mdl-20003157

ABSTRACT

The spectroscopic and kinetic studies of the interaction between bacteriorhodopsin in the M-intermediate and several surfactants (cetyl trimethyl ammonium bromide, dodecyl trimethyl ammonium bromide, diethylene glycol mono-n-hexyl ether, ethylene glycol mono-n-hexyl ether, sodium 1-decanesulfonate and sodium 1-heptanesulfonate) have been investigated using steady-state UV-VIS spectrometry and time-resolved absorption techniques. The steady-state spectral results show that bR retains its trimeric state. Time-resolved observations indicate that the rate of deprotonation of the protonated Schiff base increases in the presence of the cationic surfactants, whereas insignificant changes are observed in the neutral or anionic surfactants. The rate of the reprotonation of the Schiff base in the transition M --> N is accelerated in anionic and neutral surfactants, but is decelerated in the presence of the cationic surfactants. Surfactants with a longer hydrocarbon tail have a greater effect on the kinetics when compared with surfactants having shorter hydrocarbon tails. The opposite effect is observed when the hydrophilic head of the surfactants contains opposite charges. These distinct kinetics are discussed in terms of the difference in the modified surface hydrophilicity of the bR and the possible protein configurational changes upon surfactant treatments.


Subject(s)
Bacteriorhodopsins/metabolism , Surface-Active Agents/pharmacology , Bacteriorhodopsins/drug effects , Bacteriorhodopsins/physiology , Kinetics , Photoperiod , Protein Conformation , Schiff Bases/chemistry , Spectrum Analysis , Static Electricity , Structure-Activity Relationship , Surface-Active Agents/chemistry
8.
Biochemistry ; 48(5): 1112-22, 2009 Feb 10.
Article in English | MEDLINE | ID: mdl-19140737

ABSTRACT

We examined functional and structural roles for the bacteriorhodopsin (bR) carboxyl-terminus. The extramembranous and intracellular carboxyl-terminus was deleted by insertion of premature translation stop codons. Deletion of the carboxyl-terminus had no effect on purple membrane (PM) lattice dimensions, sheet size, or the electrogenic environment of the ground-state chromophore. Removal of the distal half of the carboxyl-terminus had no effect on light-activated proton pumping, however, truncation of the entire carboxyl-terminus accelerated the rates of M-state decay and proton uptake approximately 3.7-fold and severely distorted the kinetics of proton uptake. Differential scanning calorimetry (DSC) and SDS denaturation demonstrated that removal of the carboxyl-terminus decreased protein stability. The DSC melting temperature was lowered by 6 degrees C and the calorimetric enthalpy reduced by 50% following removal of the carboxyl-terminus. Over the time range of milliseconds to hours at least 3 phases were required to describe the SDS denaturation kinetics for each bR construction. The fastest phases were indistinguishable for all bR's, and reflected PM solubilization. At pH 7.4, 20 degrees C, and in 0.3% SDS (w/v) the half-times of bR denaturation were 19.2 min for the wild-type, 12.0 min for the half-truncation and 3.6 min for the full-truncation. Taken together the results of this study suggest that the bR ground state exhibits two "domains" of stability: (1) a core chromophore binding pocket domain that is insensitive to carboxyl-terminal interactions and (2) the surrounding helical bundle whose contributions to protein stability and proton pumping are influenced by long-range interactions with the extramembranous carboxyl-terminus.


Subject(s)
Bacteriorhodopsins/chemistry , Bacteriorhodopsins/physiology , Peptide Fragments/chemistry , Peptide Fragments/physiology , Protons , Amino Acid Sequence , Base Sequence , Cytoplasm/chemistry , Cytoplasm/metabolism , Escherichia coli/chemistry , Halobacterium salinarum/chemistry , Lipids/chemistry , Molecular Sequence Data , Protein Stability , Protein Structure, Secondary , Protein Structure, Tertiary , Static Electricity
10.
Chem Soc Rev ; 37(11): 2422-32, 2008 Nov.
Article in English | MEDLINE | ID: mdl-18949115

ABSTRACT

Interfacing functional proteins with solid supports for device applications is a promising route to possible applications in bio-electronics, -sensors, and -optics. Various possible applications of bacteriorhodopsin (bR) have been explored and reviewed since the discovery of bR. This tutorial review discusses bR as a medium for biomolecular optoelectronics, emphasizing ways in which it can be interfaced, especially as a thin film, solid-state current-carrying electronic element.


Subject(s)
Bacteriorhodopsins , Biosensing Techniques/methods , Electric Conductivity , Electronics/methods , Bacteriorhodopsins/chemistry , Bacteriorhodopsins/physiology , Electrochemical Techniques , Electrodes , Immobilized Proteins/chemistry , Models, Molecular , Photochemical Processes
11.
J Opt Soc Am A Opt Image Sci Vis ; 25(3): 685-91, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18311238

ABSTRACT

Anisotropic gratings are recorded on bacteriorhodopsin films by two parallelly polarized beams, and the effect of the polarization orientation of the reconstructing beam on the diffraction efficiency kinetics is studied. A theoretical model for the diffraction efficiency kinetics of the anisotropic grating is developed by combining Jones-matrix and photochromic two-state theory. It is found that the polarization azimuth of the reconstructing beam produces a cosine modulation on the kinetics of the diffraction efficiency, being positive at the peak efficiency and negative for steady state. By adding auxiliary violet light during grating formation, the saturation of the grating can be restrained. As a result, the negative cosine modulation for the steady-state diffraction efficiency changes to a positive one. In addition, the steady-state diffraction efficiency is increased appreciably for all reconstructing polarization orientations.


Subject(s)
Bacteriorhodopsins/chemistry , Image Processing, Computer-Assisted , Photochemistry , Anisotropy , Bacteriorhodopsins/physiology
13.
Biochim Biophys Acta ; 1768(9): 2157-63, 2007 Sep.
Article in English | MEDLINE | ID: mdl-17669358

ABSTRACT

Glycocardiolipin is an archaeal analogue of mitochondrial cardiolipin, having an extraordinary affinity for bacteriorhodopsin, the photoactivated proton pump in the purple membrane of Halobacterium salinarum. Here purple membranes have been isolated by osmotic shock from either cells or envelopes of Hbt. salinarum. We show that purple membranes isolated from envelopes have a lower content of glycocardiolipin than standard purple membranes isolated from cells. The properties of bacteriorhodopsin in the two different purple membrane preparations are compared; although some differences in the absorption spectrum and the kinetic of the dark adaptation process are present, the reduction of native membrane glycocardiolipin content does not significantly affect the photocycle (M-intermediate rise and decay) as well as proton pumping of bacteriorhodopsin. However, interaction of the pumped proton with the membrane surface and its equilibration with the aqueous bulk phase are altered.


Subject(s)
Bacteriorhodopsins/physiology , Cardiolipins/administration & dosage , Halobacterium salinarum/physiology , Proton Pumps/physiology , Purple Membrane/drug effects , Purple Membrane/physiology , Bacteriorhodopsins/drug effects , Bacteriorhodopsins/radiation effects , Dose-Response Relationship, Drug , Halobacterium salinarum/drug effects , Halobacterium salinarum/radiation effects , Light , Proton Pumps/drug effects , Proton Pumps/radiation effects , Protons , Surface Properties
14.
J Mol Biol ; 368(3): 666-76, 2007 May 04.
Article in English | MEDLINE | ID: mdl-17367807

ABSTRACT

The behavior of the D115A mutant was analyzed by time-resolved UV-Vis and Fourier transformed infrared (FTIR) spectroscopies, aiming to clarify the role of Asp115 in the intra-protein signal transductions occurring during the bacteriorhodopsin photocycle. UV-Vis data on the D115A mutant show severely desynchronized photocycle kinetics. FTIR data show a poor transmission of the retinal isomerization to the chromoprotein, evidenced by strongly attenuated helical changes (amide I), the remarkable absence of environment alterations and protonation/deprotonation events related to Asp96 and direct Schiff base (SB) protonation form the bulk. This argues for the interactions of Asp115 with Leu87 (via water molecule) and Thr90 as key elements for the effective and vectorial proton path between Asp96 and the SB, in the cytoplasmic half of bacteriorhodopsin. The results strongly suggest the presence of a regulation motif enclosed in helices C and D (Thr90-Pro91/Asp115) which drives properly the dynamics of helix C through a set of interactions. It also supports the idea that intra-helical hydrogen bonding clusters in the buried regions of transmembrane proteins can be potential elements in intra-protein signal transduction.


Subject(s)
Aspartic Acid/chemistry , Bacteriorhodopsins/chemistry , Models, Molecular , Amino Acid Motifs , Amino Acid Substitution , Aspartic Acid/genetics , Bacteriorhodopsins/genetics , Bacteriorhodopsins/physiology , Halobacterium salinarum/metabolism , Halobacterium salinarum/radiation effects , Hydrogen Bonding , Light , Protein Structure, Secondary , Protein Transport , Purple Membrane/metabolism , Purple Membrane/radiation effects , Signal Transduction , Spectroscopy, Fourier Transform Infrared , Water/metabolism
15.
J Am Chem Soc ; 129(3): 537-46, 2007 Jan 24.
Article in English | MEDLINE | ID: mdl-17227016

ABSTRACT

Sub-10-fs laser pulses are used to impulsively photoexcite bacteriorhodopsin (BR) suspensions and probe the evolution of the resulting vibrational wave packets. Fourier analysis of the spectral modulations induced by transform-limited as well as linearly chirped excitation pulses allows the delineation of excited- and ground-state contributions to the data. On the basis of amplitude and phase variations of the modulations as a function of the dispersed probe wavelength, periodic modulations in absorption above 540 nm are assigned to ground-state vibrational coherences induced by resonance impulsive Raman spectral activity (RISRS). Probing at wavelengths below 540 nm-the red edge of the intense excited-state absorption band-uncovers new vibrational features which are accordingly assigned to wave packet motions along bound coordinates on the short-lived reactive electronic surface. They consist of high- and low-frequency shoulders adjacent to the strong C=C stretching and methyl rock modes, respectively, which have ground-state frequencies of 1008 and 1530 cm-1. Brief activity centered at approximately 900 cm-1, which is characteristic of ground-state HOOP modes, and strong modulations in the torsional frequency range appear as well. Possible assignments of the bands and their implication to photoinduced reaction dynamics in BR are discussed. Reasons for the absence of similar signatures in the pump-probe spectral modulations at longer probing wavelengths are considered as well.


Subject(s)
Bacteriorhodopsins/chemistry , Photochemistry , Rhodobacter sphaeroides/physiology , Absorption , Bacteriorhodopsins/physiology , Models, Theoretical , Spectrum Analysis, Raman/methods , Time Factors
16.
Photochem Photobiol ; 83(1): 50-62, 2007.
Article in English | MEDLINE | ID: mdl-16872254

ABSTRACT

Development of bacteriorhodopsin (bR) analogues employing chromophore substitution technique for the purpose of characterizing the binding site of bR and generating bR analogues with novel opto-electronic properties for applications as photoactive element in nanotechnical devices are described. Additionally, the photophysical and photochemical properties of variously substituted diarylpolyenes as models of photobiologically relevant linear polyenes are discussed. The role of charge separated dipolar excited states in the photoprocesses of linear polyenes is highlighted.


Subject(s)
Bacteriorhodopsins/chemistry , Bacteriorhodopsins/radiation effects , Halobacterium/chemistry , Photochemistry , Polyenes/chemistry , Bacteriorhodopsins/physiology , Binding Sites , Models, Biological , Models, Chemical , Nanotechnology , Polyenes/metabolism , Stereoisomerism
17.
Eur Biophys J ; 36(3): 199-211, 2007 Mar.
Article in English | MEDLINE | ID: mdl-17186234

ABSTRACT

Comparative analysis of the photoelectric response of dried films of purple membranes (PM) depending on their degree of orientation is presented. Time dependence of the photo-induced protein electric response signal (PERS) of oriented and non-oriented films to a single laser pulse in the presence of the external electric field (EEF) was experimentally determined. The signal does not appear in the non-oriented films when the EEF is absent, whereas the PERS of the oriented PM films demonstrates the variable polarity on the microsecond time scale. In the presence of the EEF the PERS of the non-oriented film rises exponentially preserving the same polarization. The polarization of the PERS changes by changing the polarity of the EEF with no influence on the time constant of the PERS kinetics. The EEF effect on the PERS of the oriented films is more complicated. By subtracting the PERS when EEF not equal 0 from the PERS when EEF = 0 the resulting signal is comparable to that of the non-oriented films. Generalizing the experimental data we conclude that the EEF influence is of the same origin for the films of any orientation. To explain the experimental results the two-state model is suggested. It assumes that the EEF directionally changes the pK(a) values of the Schiff base (SB) and of the proton acceptor aspartic acid D85 in bacteriorhodopsin. Because of that the SB-->D85 proton transfer might be blocked and consequently the L-->M intermediate transition should vanish. Thus, on the characteristic time scale tau( L --> M ) approximately 30 micros; both intermediates, the M intermediate, appearing under normal conditions, and the L intermediate as persisting under the blocked conditions when D85 is protonated, should coexist in the film. The total PERS is a result of the potentials corresponding to the electrogenic products of intermediates L and M that are of the opposite polarity. It is concluded that the ratio of bacteriorhodopsin concentrations corresponding to the L and M intermediates is driven by the EEF and, consequently, it should define the PERS of the non-oriented films. According to this model the orientation degree of the film could be evaluated by describing the PERS.


Subject(s)
Bacteriorhodopsins/chemistry , Bacteriorhodopsins/physiology , Models, Biological , Proton Pumps/chemistry , Proton Pumps/physiology , Protons , Bacteriorhodopsins/radiation effects , Computer Simulation , Dose-Response Relationship, Radiation , Electromagnetic Fields , Light , Proton Pumps/radiation effects , Radiation Dosage
18.
Biophys J ; 91(4): L29-31, 2006 Aug 15.
Article in English | MEDLINE | ID: mdl-16782795

ABSTRACT

Cell penetrating peptides (CPPs) are small peptides that are able to penetrate the plasma membrane of mammalian cells. Because these peptides can also carry large hydrophilic cargos such as proteins, they could potentially be used to transport biologically active drugs across cell membranes to modulate in vivo biology. One characteristic feature of the CPPs is that they typically have a net positive charge. Therefore, a key issue associated with the transport mechanism is the role of the transmembrane electrochemical potential in driving the peptides across the membrane. In this study, we have reconstituted bacteriorhodopsin (bR) in large unilamellar vesicles (LUVs) with fluorescein-labeled CPP penetratin enclosed within the LUVs under conditions when the fluorescence is quenched. Illumination of the bacteriorhodopsin-containing LUVs resulted in creation of a transmembrane proton electrochemical gradient (positive on the inside). Upon generation of this gradient, an increase in fluorescence was observed, which shows that the proton gradient drives the translocation of penetratin. The mechanism most likely can be generalized to other CPPs.


Subject(s)
Bacteriorhodopsins/physiology , Carrier Proteins/metabolism , Cell Membrane/physiology , Peptides/metabolism , Protein Transport/physiology , Proton Pumps/physiology , Bacteriorhodopsins/radiation effects , Cell Membrane/radiation effects , Cell-Penetrating Peptides , Computer Systems , Light
19.
Mol Microbiol ; 55(6): 1681-94, 2005 Mar.
Article in English | MEDLINE | ID: mdl-15752193

ABSTRACT

In Halobacterium salinarum mutants containing either of the light-driven ion pumps bacteriorhodopsin (H(+)) or halorhodopsin (Cl(-)) as their only retinal protein, a decrease of irradiance in the absence of respiration causes a phototactic response. The conversion of the causal event, a decrease of proton motive force across the cell membrane, into a reversal of flagellar motor rotational direction was expected to involve a transducer. Via deletion analysis of all 18 known and putative halobacterial transducer (htr) genes, we found that Htr14, a methylatable membrane-bound transducer lacking an extracellular domain, mediates the biological response, which includes adaptive methylation. Based on a minimal stimulus length of 200 ms and the determined cytoplasmic buffering capacity, we conclude that the change in the membrane potential (DeltaPsi), and not that of the internal pH, is the signal-generating event. Htr14 was therefore renamed to Membrane potential change Transducer, or MpcT. It is the first transducer for which the causative stimulus could be narrowed to a change in DeltaPsi, as opposed to a change in pH or cellular redox state.


Subject(s)
Archaeal Proteins/physiology , Halobacterium salinarum/physiology , Ion Pumps/physiology , Membrane Proteins/physiology , Adaptation, Physiological , Archaeal Proteins/genetics , Bacteriorhodopsins/physiology , Biological Transport , Flagella/physiology , Gene Deletion , Genes, Archaeal , Ion Pumps/genetics , Membrane Potentials , Membrane Proteins/genetics , Movement , Sequence Deletion , Signal Transduction
20.
Opt Lett ; 29(19): 2264-6, 2004 Oct 01.
Article in English | MEDLINE | ID: mdl-15524375

ABSTRACT

A monolithically integrated bacteriorhodopsin-semiconductor phototransceiver is demonstrated for the first time to the authors' knowledge. In this novel biophotonic optical interconnect, the input photoexcitation is detected by bacteriorhodopsin (bR) that has been selectively deposited onto the gate of a GaAs-based field-effect transistor. The photovoltage developed across the bR is converted by the transistor into an amplified photocurrent, which drives an integrated light-emitting diode with a Ga0.37Al0.63As active region. Advantage is taken of the high-input impedance of the field-effect transistor, which matches the high internal resistance of bR. The input and output wavelengths are 594 and 655 nm, respectively. The transient response of the optoelectronic circuit to modulated input light has also been studied.


Subject(s)
Amplifiers, Electronic , Bacteriorhodopsins/chemistry , Bacteriorhodopsins/radiation effects , Biosensing Techniques/instrumentation , Electrochemistry/instrumentation , Nanotechnology/instrumentation , Photochemistry/instrumentation , Aluminum Compounds , Arsenicals , Bacteriorhodopsins/physiology , Biosensing Techniques/methods , Dose-Response Relationship, Radiation , Electrochemistry/methods , Equipment Design , Equipment Failure Analysis , Gallium , Nanotechnology/methods , Photochemistry/methods , Systems Integration , Transistors, Electronic
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