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In Vivo Photocycle of the Euglena gracilis Photoreceptor

Barsanti, Laura; Passarelli, Vincenzo; Walne, Patricia L.; Gualtieri, Paolo
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /02/1997 Português
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We present the light-induced photocycle of the paraflagellar swelling of Euglena gracilis. The kinetics of this process was reconstructed by sampling its fluorescence emission and switching the excitation light from 365 nm to 436 nm. Stable intermediates in the photocycle were manifested. The measured millisecond resolution kinetics best fits a Michaelis-Menten equation. The data provide strong evidence that the paraflagellar swelling, a three-dimensional natural crystal of a light-detecting protein, is the true Euglena photoreceptor.

Kinetic model of primary energy transfer and trapping in photosynthetic membranes

Pullerits, Tõnu; Freiberg, Arvi
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /10/1992 Português
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The picosecond time-domain incoherent singlet excitation transfer and trapping kinetics in core antenna of photosynthetic bacteria are studied in case of low excitation intensities by numerical integration of the appropriate master equation in a wide temperature range of 4-300 K. The essential features of our two-dimensional-lattice model are as follows: Förster excitation transfer theory, spectral heterogeneity of both the light-harvesting antenna and the reaction center, treatment of temperature effects through temperature dependence of spectral bands, inclusion of inner structure of the trap, and transition dipole moment orientation. The fluorescence kinetics is analyzed in terms of distributions of various kinetic components, and the influence of different inhomogeneities (orientational, spectral) is studied.

On the long-wavelength component of the light-harvesting complex of some photosynthetic bacteria

Fischer, Monika R.; Hoff, Arnold J.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /10/1992 Português
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The effect of the presence of a minor antenna component in light-harvesting complexes of photosynthetic bacteria is investigated with numerical simulation employing the transition probability matrix method. A model antenna system of hexagonal symmetry is adopted, using as a working hypothesis that the minor component forms a ring around the trap. Three cases have been considered: (a) the minor component is isoenergetic with the trap, which is at lower energy than the antennas (the “supertrap”), (b) the minor component is at lower energy than the trap, which is at lower energy than the antennas (the “asymmetric gutter”), (c) the minor component is at lower energy than the trap, which is isoenergetic with the antennas (the “gutter”). It is found that the supertrap speeds up the fluorescence decay and enhances the trapping efficiency, whereas the gutter slows down the fluorescence decay and decreases the trapping efficiency. It is concluded that, in contrast to a recent suggestion (Bergström, H., R. van Grondelle, and V. Sundström. 1989. FEBS (Fed. Eur. Biochem. Soc.) Lett. 250:503-508), concentrating excitations in the vicinity of the trap by the so-called long-wavelength minor antenna component purportedly present in Rhodobacter sphaeroides and Rhodospirillum rubrum instead of improving trapping actually impedes trapping.

Low temperature FTIR study of the Schiff base reprotonation during the M-to-bR backphotoreaction: Asp 85 reprotonates two distinct types of Schiff base species at different temperatures

Takei, H.; Gat, Y.; Sheves, M.; Lewis, A.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /12/1992 Português
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We have applied low temperature difference FTIR spectroscopy to investigate intermediates produced from the M intermediate upon blue light excitation (<480 nm). In agreement with an earlier report by Balashov and Litvin (1981), who studied these intermediates with low temperature visible absorption spectrophotometry, we have observed at least three stages in this backphotoreaction. The initial photoproduct is stable at 100 K, and two products of subsequent thermal reactions are observed upon raising the temperature to 130 and 160 K, respectively.

Time-resolved absorption and fluorescence from the bacteriorhodopsin photocycle in the nanosecond time regime

Delaney, J. K.; Brack, T. L.; Atkinson, G. H.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /05/1993 Português
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Picosecond transient absorption (PTA) in the 568-660-nm region is measured over the initial 80 ns of the bacteriorhodopsin photocycle. After photocycle initiation with 573-nm excitation (7-ps pulsewidth), these PTA data reflect the formation during the initial 40 ps of two long-recognized intermediates with red-shifted (relative to that of BR-570) absorption bands, namely J-625 and K-590. PTA signals at 568, 628, and 652 nm are unchanged for the remainder of the 80-ns photocycle interval measured, demonstrating that no other intermediates, including the proposed KL, are observable by absorption changes. Picosecond time-resolved fluorescence (PTRF), measured at 740 nm, is initiated by 7 ps excitation of the species present at various time delays after the photocycle begins. PTRF signals change rapidly over the initial 40 ps, reflecting, first, the depletion of the ground state BR-570 population and, subsequently, the formation of K-590. The PTRF signal then decreases monotonically with a time constant of 5.5 ± 0.5 ns from its maximum near a 50-ps delay until it reaches a minimum at a delay of ≈ 13 ns. For time delays between 13 and 80 ns, the PTRF signal remains unchanged and slightly higher than that measured from BR-570 alone. The rapid decrease in PTRF signals over the same photocycle interval in which the PTA signals remain unchanged suggests that the retinal-protein interactions involving electronically excited K-590 (K*) are being significantly altered.

Energy transfer and charge separation kinetics in photosystem I: Part 1: Picosecond transient absorption and fluorescence study of cyanobacterial photosystem I particles

Holzwarth, Alfred R.; Schatz, Günther; Brock, Helmuth; Bittersmann, Edith
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /06/1993 Português
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The energy transfer and charge separation kinetics of a photosystem I (PS I) core particle of an antenna size of 100 chlorophyll/P700 has been studied by combined fluorescence and transient absorption kinetics with picosecond resolution. This is the first combined picosecond study of transient absorption and fluorescence carried out on a PS I particle and the results are consistent with each other. The data were analyzed by both global lifetime and global target analysis procedures. In fluorescence major lifetime components were found to be 12 and 36 ps. The shorter-lived one shows a negative amplitude at long wavelengths and is attributed to an energy transfer process between pigments in the main antenna Chl pool and a small long-wavelength Chl pool emitting around 720 nm whereas the longer-lived component is assigned to the overall charge separation lifetime. The lifetimes resolved in transient absorption are 7-8 ps, 33 ps, and [unk]1 ns. The shortest-lived one is assigned to energy transfer between the same pigment pools as observed also in fluorescence kinetics, the middle component of 33 ps to the overall charge separation, and the long-lived component to the lifetime of the oxidized primary donor P700+. The transient absorption data indicate an even faster...

Low-Intensity Pump-Probe Measurements on the B800 Band of Rhodospirillum molischianum

Wendling, Markus; Mourik, Frank van; van Stokkum, Ivo H. M.; Salverda, Jante M.; Michel, Hartmut; Grondelle, Rienk van
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /01/2003 Português
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We have measured low-intensity, polarized one-color pump-probe traces in the B800 band of the light-harvesting complex LH2 of Rhodospirillum molischianum at 77 K. The excitation/detection wavelength was tuned through the B800 band. A single-wavelength and a global target analysis of the data were performed with a model that accounts for excitation energy transfer among the B800 molecules and from B800 to B850. By including the anisotropy of the signals into the fitting procedure, both transfer processes could be separated. It was estimated in the global target analysis that the intra-B800 energy transfer, i.e., the hopping of the excitation from one B800 to another B800 molecule, takes ∼0.5 ps at 77 K. This transfer time increases with the excitation/detection wavelength from 0.3 ps on the blue side of the B800 band to ∼0.8 ps on the red side. The residual B800 anisotropy shows a wavelength dependence as expected for energy transfer within an inhomogeneously broadened cluster of weakly coupled pigments. In the global target analysis, the transfer time from B800 to B850 was determined to be ∼1.7 ps at 77 K. In the single-wavelength analysis, a speeding-up of the B800 → B850 energy transfer rate toward the blue edge of the B800 band was found. This nicely correlates with the proposed position of the suggested high-exciton component of the B850 band acting as an additional decay channel for B800 excitations.

Energy Transfer in Light-Harvesting Complexes LHCII and CP29 of Spinach Studied with Three Pulse Echo Peak Shift and Transient Grating

Salverda, Jante M.; Vengris, Mikas; Krueger, Brent P.; Scholes, Gregory D.; Czarnoleski, Adam R.; Novoderezhkin, Vladimir; Amerongen, Herbert van; Grondelle, Rienk van
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /01/2003 Português
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Three pulse echo peak shift and transient grating (TG) measurements on the plant light-harvesting complexes LHCII and CP29 are reported. The LHCII complex is by far the most abundant light-harvesting complex in higher plants and fulfills several important physiological functions such as light-harvesting and photoprotection. Our study is focused on the light-harvesting function of LHCII and the very similar CP29 complex and reveals hitherto unresolved excitation energy transfer processes. All measurements were performed at room temperature using detergent isolated complexes from spinach leaves. Both complexes were excited in their Chl b band at 650 nm and in the blue shoulder of the Chl a band at 670 nm. Exponential fits to the TG and three pulse echo peak shift decay curves were used to estimate the timescales of the observed energy transfer processes. At 650 nm, the TG decay can be described with time constants of 130 fs and 2.2 ps for CP29, and 300 fs and 2.8 ps for LHCII. At 670 nm, the TG shows decay components of 230 fs and 6 ps for LHCII, and 300 fs and 5 ps for CP29. These time constants correspond to well-known energy transfer processes, from Chl b to Chl a for the 650 nm TG and from blue (670 nm) Chl a to red (680 nm) Chl a for the 670 nm TG. The peak shift decay times are entirely different. At 650 nm we find times of 150 fs and 0.5–1 ps for LHCII...

Vibrational Spectroscopy of an Algal Phot-LOV1 Domain Probes the Molecular Changes Associated with Blue-Light Reception

Ataka, K.; Hegemann, P.; Heberle, J.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /01/2003 Português
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The LOV1 domain of the blue light Phot1-receptor (phototropin homolog) from Chlamydomonas reinhardtii has been studied by vibrational spectroscopy. The FMN modes of the dark state of LOV1 were identified by preresonance Raman spectroscopy and assigned to molecular vibrations. By comparing the blue-light-induced FTIR difference spectrum with the preresonance Raman spectrum, most of the differences are due to FMN modes. Thus, we exclude large backbone changes of the protein that might occur during the phototransformation of the dark state LOV1-447 into the putative signaling state LOV1-390. Still, the presence of smaller amide difference bands cannot be excluded but may be masked by overlapping FMN modes. The band at 2567 cm−1 is assigned to the S-H stretching vibration of C57, the residue that forms the transient thio-adduct with the chromophore FMN. The occurrence of this band is evidence that C57 is protonated in the dark state of LOV1. This result challenges conclusions from the homologous LOV2 domain from oat that the thiolate of the corresponding cysteine is the reactive species.

Self-Regulation Phenomena Applied to Bacterial Reaction Centers: 2. Nonequilibrium Adiabatic Potential: Dark and Light Conformations Revisited

Goushcha, Alexander O.; Manzo, Anthony J.; Scott, Gary W.; Christophorov, Leonid N.; Knox, Peter P.; Barabash, Yuri M.; Kapoustina, Marina T.; Berezetska, Natalja M.; Kharkyanen, Valery N.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /02/2003 Português
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Experimental and theoretical results in support of nonlinear dynamic behavior of photosynthetic reaction centers under light-activated conditions are presented. Different conditions of light adaptation allow for preparation of reaction centers in either of two different conformational states. These states were detected both by short actinic flashes and by the switching of the actinic illumination level between different stationary state values. In the second method, the equilibration kinetics of reaction centers isolated from Rhodobacter sphaeroides were shown to be inherently biphasic. The fast and slow equilibration kinetics are shown to correspond to electron transfer (charge separation) at a fixed structure and to combined electron-conformational transitions governed by the bounded diffusion along the potential surface, respectively. The primary donor recovery kinetics after an actinic flash revealed a pronounced dependence on the time interval (Δt) between cessation of a lengthy preillumination of a sample and the actinic flash. A pronounced slow relaxation component with a decay half time of more than 50 s was measured for Δt > 10 s. This component corresponds to charge recombination in reaction centers for which light-induced structural changes have not relaxed completely before the flash. The amplitude of this component depended on the conditions of the sample preparation...

Excitation Energy Transfer Dynamics and Excited-State Structure in Chlorosomes of Chlorobium phaeobacteroides

Pšenčík, Jakub; Ma, Ying-Zhong; Arellano, Juan B.; Hála, Jan; Gillbro, Tomas
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /02/2003 Português
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The excited-state relaxation within bacteriochlorophyll (BChl) e and a in chlorosomes of Chlorobium phaeobacteroides has been studied by femtosecond transient absorption spectroscopy at room temperature. Singlet-singlet annihilation was observed to strongly influence both the isotropic and anisotropic decays. Pump intensities in the order of 1011 photons × pulse−1 × cm−2 were required to obtain annihilation-free conditions. The most important consequence of applied very low excitation doses is an observation of a subpicosecond process within the BChl e manifold (∼200–500 fs), manifesting itself as a rise in the red part of the Qy absorption band of the BChl e aggregates. The subsequent decay of the kinetics measured in the BChl e region and the corresponding rise in the baseplate BChl a is not single-exponential, and at least two components are necessary to fit the data, corresponding to several BChl e→BChl a transfer steps. Under annihilation-free conditions, the anisotropic kinetics show a generally slow decay within the BChl e band (10–20 ps) whereas it decays more rapidly in the BChl a region (∼1 ps). Analysis of the experimental data gives a detailed picture of the overall time evolution of the energy relaxation and energy transfer processes within the chlorosome. The results are interpreted within an exciton model based on the proposed structure.

Deuterium Isotope Effects in the Photocycle Transitions of the Photoactive Yellow Protein

Hendriks, Johnny; van Stokkum, Ivo H. M.; Hellingwerf, Klaas J.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /02/2003 Português
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The Photoactive Yellow Protein (PYP) from Halorhodospira halophila (formerly Ectothiorhodospira halophila) is increasingly used as a model system. As such, a thorough understanding of the photocycle of PYP is essential. In this study we have combined information from pOH- (or pH-) dependence and (kinetic) deuterium isotope effects to elaborate on existing photocycle models. For several characteristics of PYP we were able to make a distinction between pH- and pOH-dependence, a nontrivial distinction when comparing data from samples dissolved in H2O and D2O. It turns out that most characteristics of PYP are pOH-dependent. We confirmed the existence of a pB′ intermediate in the pR to pB transition of the photocycle. In addition, we were able to show that the pR to pB′ transition is reversible, which explains the previously observed biexponential character of the pR-to-pB photocycle step. Also, the absorption spectrum of pB′ is slightly red-shifted with respect to pB. The recovery of the pG state is accompanied by an inverse kinetic deuterium isotope effect. Our interpretation of this is that before the chromophore can be isomerized, it is deprotonated by a hydroxide ion from solution. From this we propose a new photocycle intermediate...

Phot-LOV1: Photocycle of a Blue-Light Receptor Domain from the Green Alga Chlamydomonas reinhardtii

Kottke, Tilman; Heberle, Joachim; Hehn, Dominic; Dick, Bernhard; Hegemann, Peter
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /02/2003 Português
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The “Phot” protein family comprises blue-light photoreceptors that consist of two flavin mononucleotide (FMN)-binding LOV (light, oxygen, and voltage) domains and a serine/threonine kinase domain. We have investigated the LOV1 domain of Phot1 from Chlamydomonas reinhardtii by time-resolved absorption spectroscopy. Photoexcitation of the dark form, LOV1-447, causes transient bleaching and formation of two spectrally similar red-shifted intermediates that are both assigned to triplet states of the FMN. The triplet states decay with time constants of 800 ns and 4 μs with an efficiency of >90% into a blue-shifted intermediate, LOV1-390, that is attributed to a thiol adduct of cysteine 57 to FMN C(4a). LOV1-390 reverts to the dark form in hundreds of seconds, the time constant being dependent on pH and salt concentration. In the mutant C57S, where the thiol adduct cannot be formed, the triplet state displays an oxygen-dependent decay directly to the dark form. We present here a spectroscopic characterization of an algal sensory photoreceptor in general and of a LOV1 domain photocycle in particular. The results are discussed with respect to the behavior of the homologous LOV2 domain from oat.

Characterization of the Photochemical Reaction Cycle of Proteorhodopsin

Váró, György; Brown, Leonid S.; Lakatos, Melinda; Lanyi, Janos K.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /02/2003 Português
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Absorption changes in the photocycle of the recently described retinal protein, proteorhodopsin, are analyzed. The transient spectra at pH 9.5, where it acts as a light-driven proton pump, reveal the existence of three spectrally different intermediates, K, M, and N, named in analogy with the photointermediates of bacteriorhodopsin. Model analysis based on time-dependent absorption kinetic signals at four wavelengths suggested the existence of two more spectrally silent intermediates and lead to a sequential reaction scheme with five intermediates, K, M1, M2, N, and PR′, before decay to the initial state PR. An L-like intermediate was not observed, probably for kinetic reasons. By measuring the light-generated electric signal of an oriented sample, the electrogenicity of each intermediate could be determined. The electrogenicities of the first three intermediates (K, M1, and M2) have small negative value, but the last three components, corresponding to the N and PR′ intermediates and PR, are positive and two-orders-of-magnitude larger. These states give the major contributions to the proton translocation across the membrane. The energetic scheme of the photocycle was calculated from the temperature-dependence of the absorption kinetic signals.

Time-Resolved FTIR Studies of Sensory Rhodopsin II (NpSRII) from Natronobacterium pharaonis: Implications for Proton Transport and Receptor Activation

Hein, Michael; Wegener, Ansgar A.; Engelhard, Martin; Siebert, Friedrich
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /02/2003 Português
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The photocycle of the photophobic receptor from Natronobacterium pharaonis, NpSRII, is studied by static and time-resolved step-scan Fourier transform infrared spectroscopy. Both low-temperature static and time-resolved spectra resolve a K-like intermediate, and the corresponding spectra show little difference within the noise of the time-resolved data. As compared to intermediate K of bacteriorhodopsin, relatively large amide I bands indicate correspondingly larger distortions of the protein backbone. The time-resolved spectra identify an intermediate L-like state with surprisingly small additional molecular alterations. With the formation of intermediate M, the Schiff-base proton is transferred to the counterion Asp-75. This state is characterized by larger amide bands indicating larger distortions of the protein. We can identify a second M state that differs only in small-protein bands. Reisomerization of the chromophore to all-trans occurs with the formation of intermediate O. The accelerated decay of intermediate M caused by azide results in another red-shifted intermediate with a protonated Schiff base. The chromophore in this state, however, still has 13-cis geometry. Nevertheless, the reisomerization is still as slow as under the conditions without azide. The results are discussed with respect to mechanisms of the observed proton pumping and the possible roles of the intermediates in receptor activation.

Crystal Structures and Molecular Mechanism of a Light-Induced Signaling Switch: The Phot-LOV1 Domain from Chlamydomonas reinhardtii

Fedorov, Roman; Schlichting, Ilme; Hartmann, Elisabeth; Domratcheva, Tatjana; Fuhrmann, Markus; Hegemann, Peter
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /04/2003 Português
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Phot proteins (phototropins and homologs) are blue-light photoreceptors that control mechanical processes like phototropism, chloroplast relocation, or guard-cell opening in plants. Phot receptors consist of two flavin mononucleotide (FMN)-binding light, oxygen, or voltage (LOV) domains and a C-terminal serine/threonine kinase domain. We determined crystal structures of the LOV1 domain of Phot1 from the green alga Chlamydomonas reinhardtii in the dark and illuminated state to 1.9 Å and 2.8 Å resolution, respectively. The structure resembles that of LOV2 from Adiantum (Crosson, S. and K. Moffat. 2001. Proc. Natl. Acad. Sci. USA. 98:2995–3000). In the resting dark state of LOV1, the reactive Cys-57 is present in two conformations. Blue-light absorption causes formation of a proposed active signaling state that is characterized by a covalent bond between the flavin C4a and the thiol of Cys-57. There are differences around the FMN chromophore but no large overall conformational changes. Quantum chemical calculations based on the crystal structures revealed the electronic distribution in the active site during the photocycle. The results suggest trajectories for electrons, protons, and the active site cysteine and offer an interpretation of the reaction mechanism.

Analysis of the Mode-Specific Excited-State Energy Distribution and Wavelength-Dependent Photoreaction Quantum Yield in Rhodopsin

Kim, Judy E.; Tauber, Michael J.; Mathies, Richard A.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /04/2003 Português
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The photoreaction quantum yield of rhodopsin is wavelength dependent: φ(λ) is reduced by up to 5% at wavelengths to the red of 500 nm but is invariant (φ = 0.65 ± 0.01) between 450 and 500 nm (Kim et al., 2001). To understand this nonstatistical internal conversion process, these results are compared with predictions of a Landau-Zener model for dynamic curve crossing. The initial distribution of excess photon energy in the 28 Franck-Condon active vibrational modes of rhodopsin is defined by a fully thermalized sum-over-states vibronic calculation. This calculation reveals that absorption by high-frequency unreactive modes (e.g., C=C stretches) increases as the excitation wavelength is shifted from 570 to 450 nm whereas relatively less energy is deposited into reactive low-frequency modes. This result qualitatively explains the experimentally observed wavelength dependence of φ(λ) for rhodopsin and reveals the importance of delocalized, torsional modes in the reactive pathway.

High-Performance Photovoltaic Behavior of Oriented Purple Membrane Polymer Composite Films

Zhang, Liangmin; Zeng, Tingying; Cooper, Kristie; Claus, Richard O.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /04/2003 Português
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The photovoltaic behavior of films in which bacteriorhodopsin molecules are embedded in a polyvinyl alcohol matrix has been investigated by using both pulsed laser excitation and regular light illumination. Response times as short as milliseconds, photocurrents as great as 120 μA/cm2, and photovoltages as large as 3.8 V have been obtained. A theoretical model has been developed and used to extract several physical parameters and fit the experimental results. Some important intrinsic parameters have been obtained. Theoretical results indicate that the average displacement of the excited protons is on the order of several tens of microns. Other curve fits show that photocurrent and photovoltage increase linearly with external field, but increase exponentially with flash power. These theoretical models and results can be extended to other kinds of photoactive polymeric materials.

Chlorophyll b to Chlorophyll a Energy Transfer Kinetics in the CP29 Antenna Complex: A Comparative Femtosecond Absorption Study between Native and Reconstituted Proteins

Croce, Roberta; Müller, Marc G.; Bassi, Roberto; Holzwarth, Alfred R.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /04/2003 Português
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The energy transfer processes between Chls b and Chls a have been studied in the minor antenna complex CP29 by femtosecond transient absorption spectroscopy. Two samples were analyzed: the native CP29, purified from higher plants, and the recombinant one, reconstituted in vitro with the full pigment complement. The measurements indicate that the transfer kinetics in the two samples are virtually identical, confirming that the reconstituted CP29 has the same spectroscopic properties as the native one. In particular, three lifetimes (150 fs, 1.2 ps, and 5–6 ps) were identified for Chl b-652 nm to Chl a energy transfer and at least one for Chl b-640 nm (600–800 fs). Considering that the complexes bind two Chls b per polypeptide, the observation of more than two lifetimes for the Chl b to Chl a energy transfer, in both samples, clearly indicates the presence of the so-called mixed Chl binding sites—sites which are not selective for Chl a or Chl b, but can accommodate either species. The kinetic components and spectra are assigned to specific Chl binding sites in the complex, which provides further information on the structural organization.

Energy Transfer Pathways in the Minor Antenna Complex CP29 of Photosystem II: A Femtosecond Study of Carotenoid to Chlorophyll Transfer on Mutant and WT Complexes

Croce, Roberta; Müller, Marc G.; Caffarri, Stefano; Bassi, Roberto; Holzwarth, Alfred R.
Fonte: Biophysical Society Publicador: Biophysical Society
Tipo: Artigo de Revista Científica
Publicado em /04/2003 Português
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The energy transfer processes between carotenoids and Chls have been studied by femtosecond transient absorption in the CP29-WT complex, which contains only two carotenoids per polypeptide located in the L1 and L2 sites, and in the CP29-E166V mutant in which only the L1 site is occupied. The comparison of these two samples allowed us to discriminate between the energy transfer pathways from the two carotenoid binding sites and thus to obtain detailed information on the Chl organization in CP29 and to assign the acceptor chlorophylls. For both samples, the main transfer occurs from the S2 state of the carotenoid. In the case of the L1 site the energy acceptor is the Chl a 680 nm (A2), whereas the Chl a 675 nm (A4–A5) and the Chl b 652 nm (B6) are the acceptors from the xanthophyll in the L2 site. These transfers occur with lifetimes of 80–130 fs. Two additional transfers are observed with 700-fs and 8- to 20-ps lifetimes. Both these transfers originate from the carotenoid S1 states. The faster lifetime is due to energy transfer from a vibrationally unrelaxed S1 state, whereas the 8- to 20-ps component is due to a transfer from the S1,0 state of violaxanthin and/or neoxanthin located in site L2. A comparison between the carotenoid to Chl energy transfer pathways in CP29 and LHCII is presented and differences in the structural organization in the two complexes are discussed.