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1.
Water Sci Technol ; 82(6): 1193-1204, 2020 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-33055409

RESUMO

In this paper, the energy transfer phenomena of a secondary facultative lagoon and its relationship with environmental conditions such as wind and solar radiation were studied. To this end, a three-dimensional computational fluid dynamics model was constructed within a conventional facultative lagoon located in the municipality of Ginebra-Valle del Cauca, Colombia. The model included the transport of suspended solids from inlet to outlet, the penetration of incident solar radiation into the body of water, surface wind, the transfer of heat through lateral walls and the temperature profiles of the wastewater. The model was validated using tracer studies and experimental temperature data. This demonstrated that simulated data of temperature and solar radiation penetration have an acceptable degree of consistency compared with the experimental data. The model demonstrated that temperature profiles were significantly affected by the wind at 0.45 m and 1.40 m depth, while no effect on the surface was obtained.


Assuntos
Águas Residuárias , Vento , Colômbia , Transferência de Energia , Temperatura
2.
Science ; 369(6506)2020 Aug 21.
Artigo em Inglês | MEDLINE | ID: mdl-32820091

RESUMO

Oxygenic photosynthesis is the main process that drives life on earth. It starts with the harvesting of solar photons that, after transformation into electronic excitations, lead to charge separation in the reaction centers of photosystems I and II (PSI and PSII). These photosystems are large, modular pigment-protein complexes that work in series to fuel the formation of carbohydrates, concomitantly producing molecular oxygen. Recent advances in cryo-electron microscopy have enabled the determination of PSI and PSII structures in complex with light-harvesting components called "supercomplexes" from different organisms at near-atomic resolution. Here, we review the structural and spectroscopic aspects of PSI and PSII from plants and algae that directly relate to their light-harvesting properties, with special attention paid to the pathways and efficiency of excitation energy transfer and the regulatory aspects.


Assuntos
Proteínas de Algas/química , Clorófitas/enzimologia , Oxigênio/farmacologia , Fotossíntese , Complexo de Proteína do Fotossistema I/química , Complexo de Proteína do Fotossistema II/química , Microscopia Crioeletrônica , Transferência de Energia , Oxigênio/metabolismo , Fótons
3.
Nat Commun ; 11(1): 4316, 2020 08 28.
Artigo em Inglês | MEDLINE | ID: mdl-32859932

RESUMO

Plants utilize a UV-B (280 to 315 nm) photoreceptor UVR8 (UV RESISTANCE LOCUS 8) to sense environmental UV levels and regulate gene expression to avoid harmful UV effects. Uniquely, UVR8 uses intrinsic tryptophan for UV-B perception with a homodimer structure containing 26 structural tryptophan residues. However, besides 8 tryptophans at the dimer interface to form two critical pyramid perception centers, the other 18 tryptophans' functional role is unknown. Here, using ultrafast fluorescence spectroscopy, computational methods and extensive mutations, we find that all 18 tryptophans form light-harvesting networks and funnel their excitation energy to the pyramid centers to enhance light-perception efficiency. We determine the timescales of all elementary tryptophan-to-tryptophan energy-transfer steps in picoseconds to nanoseconds, in excellent agreement with quantum computational calculations, and finally reveal a significant leap in light-perception quantum efficiency from 35% to 73%. This photoreceptor is the first system discovered so far, to be best of our knowledge, using natural amino-acid tryptophans to form networks for both light harvesting and light perception.


Assuntos
Proteínas de Arabidopsis/química , Proteínas de Arabidopsis/metabolismo , Proteínas Cromossômicas não Histona/química , Proteínas Cromossômicas não Histona/metabolismo , Fotorreceptores de Plantas/química , Fotorreceptores de Plantas/metabolismo , Arabidopsis/metabolismo , Arabidopsis/fisiologia , Arabidopsis/efeitos da radiação , Proteínas de Arabidopsis/genética , Proteínas Cromossômicas não Histona/genética , Transferência de Energia , Fluorescência , Cinética , Luz , Modelos Moleculares , Mutação , Conformação Proteica , Multimerização Proteica , Triptofano/metabolismo , Raios Ultravioleta
4.
Science ; 368(6498): 1490-1495, 2020 06 26.
Artigo em Inglês | MEDLINE | ID: mdl-32587021

RESUMO

Photosynthesis achieves near unity light-harvesting quantum efficiency yet it remains unknown whether there exists a fundamental organizing principle giving rise to robust light harvesting in the presence of dynamic light conditions and noisy physiological environments. Here, we present a noise-canceling network model that relates noisy physiological conditions, power conversion efficiency, and the resulting absorption spectra of photosynthetic organisms. Using light conditions in full solar exposure, light filtered by oxygenic phototrophs, and light filtered under seawater, we derived optimal absorption characteristics for efficient solar power conversion. We show how light-harvesting antennae can be tuned to maximize power conversion efficiency by minimizing excitation noise, thus providing a unified theoretical basis for the observed wavelength dependence of absorption in green plants, purple bacteria, and green sulfur bacteria.


Assuntos
Complexos de Proteínas Captadores de Luz/fisiologia , Fotossíntese , Plantas/metabolismo , Proteobactérias/metabolismo , Adsorção , Chlorobi , Transferência de Energia , Luz , Oxigênio , Energia Solar
5.
Nat Commun ; 11(1): 2460, 2020 05 18.
Artigo em Inglês | MEDLINE | ID: mdl-32424138

RESUMO

Fluorescent barcoding is a pivotal technique for the investigation of the microscale world, from information storage to the monitoring of dynamic biochemical processes. Using fluorescence lifetime as the readout modality offers more reproducible and quantitative outputs compared to conventional fluorescent barcoding, being independent of sample concentration and measurement methods. However, the use of fluorescence lifetime in this area has been limited by the lack of strategies that provide spatiotemporal manipulation of the coding process. In this study, we design a two-component photo-switchable nanogel that exhibits variable fluorescence lifetime upon photoisomerization-induced energy transfer processes through light irradiation. This remotely manipulated fluorescence lifetime property could be visually mapped using fluorescence lifetime imaging microscopy (FLIM), allowing selective storage and display of information at the microscale. Most importantly, the reversibility of this system further provides a strategy for minimizing the background influence in fluorescence lifetime imaging of live cells and sub-cellular organelles.


Assuntos
Luz , Microscopia de Fluorescência/métodos , Células A549 , Sobrevivência Celular , Transferência de Energia , Fluorescência , Humanos , Isomerismo , Mitocôndrias/metabolismo , Nanogéis/química , Polietilenoglicóis/química , Polietilenoimina/química , Polímeros/química , Frações Subcelulares
6.
Nat Commun ; 11(1): 2481, 2020 05 18.
Artigo em Inglês | MEDLINE | ID: mdl-32424145

RESUMO

Photosynthetic light-harvesting complexes (LHCs) play a pivotal role in collecting solar energy for photochemical reactions in photosynthesis. One of the major LHCs are fucoxanthin chlorophyll a/c-binding proteins (FCPs) present in diatoms, a group of organisms having important contribution to the global carbon cycle. Here, we report a 2.40-Å resolution structure of the diatom photosystem I (PSI)-FCPI supercomplex by cryo-electron microscopy. The supercomplex is composed of 16 different FCPI subunits surrounding a monomeric PSI core. Each FCPI subunit showed different protein structures with different pigment contents and binding sites, and they form a complicated pigment-protein network together with the PSI core to harvest and transfer the light energy efficiently. In addition, two unique, previously unidentified subunits were found in the PSI core. The structure provides numerous insights into not only the light-harvesting strategy in diatom PSI-FCPI but also evolutionary dynamics of light harvesters among oxyphototrophs.


Assuntos
Diatomáceas/metabolismo , Complexos de Proteínas Captadores de Luz/química , Complexos de Proteínas Captadores de Luz/metabolismo , Complexo de Proteína do Fotossistema I/química , Complexo de Proteína do Fotossistema I/metabolismo , Clorofila/metabolismo , Proteínas de Ligação à Clorofila/química , Proteínas de Ligação à Clorofila/ultraestrutura , Transferência de Energia , Complexos de Proteínas Captadores de Luz/ultraestrutura , Modelos Moleculares , Complexo de Proteína do Fotossistema I/ultraestrutura , Ligação Proteica , Subunidades Proteicas/metabolismo , Relação Estrutura-Atividade
7.
PLoS One ; 15(3): e0230344, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32214330

RESUMO

In age-related macular degeneration (AMD) or diabetic retinopathy (DR), hypoxia and inflammatory processes lead to an upregulation of the vascular endothelial growth factor (VEGF) expression and thereby to pathological neovascularisation with incorrectly formed vessels prone to damage, thus increasing the vascular permeability and the risk of bleeding and oedema in the retina. State of the art treatment is the repeated intraocular injection of anti-VEGF molecules. For developing improved individualized treatment approaches, a minimally invasive, repeatable method for in vivo quantification of VEGF in the eye is necessary. Therefore, we designed single molecule eBRET2 VEGF biosensors by directly fusing a Renilla luciferase mutant (Rluc8) N-terminal and a green fluorescent protein (GFP2) C-terminal to a VEGF binding domain. In total, 10 different VEGF biosensors (Re01- Re10) were generated based on either single domains or full length of VEGF receptor 1 or 2 extracellular regions as VEGF binding domains. Full length expression of the biosensors in HEK293-T cells was verified via Western Blot employing an anti-Rluc8-IgG. Expression of alternative splice variants was eliminated through the deletion of the donor splice site by introduction of a silent point mutation. In all ten biosensors the energy transfer from the Rluc8 to the GFP2 occurs and generates a measurable eBRET2 ratio. Four biosensors show a relevant change of the BRET ratio (ΔBR) after VEGF binding. Furthermore, each biosensor shows a unique detection range for VEGF quantification and especially Re06 and Re07 have a high sensitivity in the range of in vivo VEGF concentrations in the eye, previously measured by invasive methods. In conclusion, we generated several eBRET2 biosensors that are suitable for VEGF quantification in vitro and could identify two eBRET2 biosensors, which may be suitable for non-invasive in vivo VEGF quantification with an implantable device.


Assuntos
Técnicas Biossensoriais/instrumentação , Medições Luminescentes/instrumentação , Proteínas Recombinantes de Fusão/química , Fator A de Crescimento do Endotélio Vascular/análise , Animais , Córnea/patologia , Retinopatia Diabética/diagnóstico , Retinopatia Diabética/patologia , Transferência de Energia , Proteínas de Fluorescência Verde/química , Proteínas de Fluorescência Verde/genética , Células HEK293 , Células Endoteliais da Veia Umbilical Humana , Humanos , Luciferases de Renilla/química , Luciferases de Renilla/genética , Degeneração Macular/diagnóstico , Degeneração Macular/patologia , Ligação Proteica , Domínios Proteicos , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Retina/patologia , Transfecção , Regulação para Cima , Fator A de Crescimento do Endotélio Vascular/metabolismo , Receptor 1 de Fatores de Crescimento do Endotélio Vascular/genética , Receptor 1 de Fatores de Crescimento do Endotélio Vascular/metabolismo
8.
Biochim Biophys Acta Bioenerg ; 1861(5-6): 148183, 2020 06 01.
Artigo em Inglês | MEDLINE | ID: mdl-32173384

RESUMO

Photosynthetic organisms are frequently exposed to excess light conditions and hence to photo-oxidative stress. To counteract photo-oxidative damage, land plants and most algae make use of non- photochemical quenching (NPQ) of excess light energy, in particular the rapidly inducible and relaxing qE-mechanism. In vascular plants, the constitutively active PsbS protein is the key regulator of qE. In the green algae C. reinhardtii, however, qE activation is only possible after initial high-light (HL) acclimation for several hours and requires the synthesis of LHCSR proteins which act as qE regulators. The precise function of PsbS, which is transiently expressed during HL acclimation in C. reinhardtii, is still unclear. Here, we investigated the impact of different PsbS amounts on HL acclimation characteristics of C. reinhardtii cells. We demonstrate that lower PsbS amounts negatively affect HL acclimation at different levels, including NPQ capacity, electron transport characteristics, antenna organization and morphological changes, resulting in an overall increased HL sensitivity and lower vitality of cells. Contrarily, higher PsbS amounts do not result in a higher NPQ capacity, but nevertheless provide higher fitness and tolerance towards HL stress. Strikingly, constitutively expressed PsbS protein was found to be degraded during HL acclimation. We propose that PsbS is transiently required during HL acclimation for the reorganization of thylakoid membranes and/or antenna proteins along with the activation of NPQ and adjustment of electron transfer characteristics, and that degradation of PsbS is essential in the fully HL acclimated state.


Assuntos
Proteínas de Algas/metabolismo , Chlamydomonas reinhardtii/metabolismo , Chlamydomonas reinhardtii/efeitos da radiação , Transferência de Energia , Luz , Substâncias Protetoras/metabolismo , Proteínas de Algas/ultraestrutura , Chlamydomonas reinhardtii/ultraestrutura , Processos Fotoquímicos , Complexo de Proteína do Fotossistema I/metabolismo , Complexo de Proteína do Fotossistema II/metabolismo , Espécies Reativas de Oxigênio/metabolismo , Tilacoides/metabolismo
9.
Biochim Biophys Acta Bioenerg ; 1861(5-6): 148115, 2020 06 01.
Artigo em Inglês | MEDLINE | ID: mdl-32204904

RESUMO

Green plants protect against photodamage by dissipating excess energy in a process called non-photochemical quenching (NPQ). In vivo, NPQ is activated by a drop in the luminal pH of the thylakoid membrane that triggers conformational changes of the antenna complexes, which activate quenching channels. The drop in pH also triggers de-epoxidation of violaxanthin, one of the carotenoids bound within the antenna complexes, into zeaxanthin, and so the amplitude of NPQ in vivo has been shown to increase in the presence of zeaxanthin. In vitro studies on light-harvesting complex II (LHCII), the major antenna complex in plants, compared different solubilization environments, which give rise to different levels of quenching and so partially mimic NPQ in vivo. However, in these studies both completely zeaxanthin-independent and zeaxanthin-dependent quenching have been reported, potentially due to the multiplicity of solubilization environments. Here, we characterize the zeaxanthin dependence of the photophysics in LHCII in a near-physiological membrane environment, which produces slightly enhanced quenching relative to detergent solubilization, the typical in vitro environment. The photophysical pathways of dark-adapted and in vitro de-epoxidized LHCIIs are compared, representative of the low-light and high-light conditions in vivo, respectively. The amplitude of quenching as well as the dissipative photophysics are unaffected by zeaxanthin at the level of individual LHCIIs, suggesting that zeaxanthin-dependent quenching is independent of the channels induced by the membrane. Furthermore, our results demonstrate that additional factors beyond zeaxanthin incorporation in LHCII are required for full development of NPQ.


Assuntos
Membrana Celular/metabolismo , Membrana Celular/efeitos da radiação , Complexos de Proteínas Captadores de Luz/metabolismo , Luz , Zeaxantinas/metabolismo , Carotenoides/metabolismo , Clorofila/metabolismo , Transferência de Energia , Fluorescência , Concentração de Íons de Hidrogênio , Modelos Moleculares , Spinacia oleracea/metabolismo , Zeaxantinas/química
10.
Biochim Biophys Acta Bioenerg ; 1861(7): 148187, 2020 07 01.
Artigo em Inglês | MEDLINE | ID: mdl-32173383

RESUMO

Phycobilisomes (PBs) absorb light and supply downstream photosynthetic processes with excitation energy in many cyanobacteria and algae. In response to a sudden increase in light intensity, excess excitation energy is photoprotectively dissipated in PBs by means of the orange carotenoid protein (OCP)-related mechanism or via a light-activated intrinsic decay channel. Recently, we have identified that both mechanisms are associated with far-red emission states. Here, we investigate the far-red states involved with the light-induced intrinsic mechanism by exploring the energy landscape and electro-optical properties of the pigments in PBs. While Stark spectroscopy showed that the far-red states in PBs exhibit a strong charge-transfer (CT) character at cryogenic temperatures, single molecule spectroscopy revealed that CT states should also be present at room temperature. Owing to the strong environmental sensitivity of CT states, the knowledge gained from this study may contribute to the design of a new generation of fluorescence markers.


Assuntos
Transferência de Energia , Ficobilissomas/metabolismo , Conformação Proteica , Imagem Individual de Molécula , Espectrometria de Fluorescência , Synechocystis/metabolismo , Temperatura
11.
Biochim Biophys Acta Bioenerg ; 1861(7): 148191, 2020 07 01.
Artigo em Inglês | MEDLINE | ID: mdl-32201306

RESUMO

Light-harvesting complex II (LHCII) from the marine green macroalga Bryopsis corticulans is spectroscopically characterized to understand the structural and functional changes resulting from adaptation to intertidal environment. LHCII is homologous to its counterpart in land plants but has a different carotenoid and chlorophyll (Chl) composition. This is reflected in the steady-state absorption, fluorescence, linear dichroism, circular dichroism and anisotropic circular dichroism spectra. Time-resolved fluorescence and two-dimensional electronic spectroscopy were used to investigate the consequences of this adaptive change in the pigment composition on the excited-state dynamics. The complex contains additional Chl b spectral forms - absorbing at around 650 nm and 658 nm - and lacks the red-most Chl a forms compared with higher-plant LHCII. Similar to plant LHCII, energy transfer between Chls occurs on timescales from under hundred fs (mainly from Chl b to Chl a) to several picoseconds (mainly between Chl a pools). However, the presence of long-lived, weakly coupled Chl b and Chl a states leads to slower exciton equilibration in LHCII from B. corticulans. The finding demonstrates a trade-off between the enhanced absorption of blue-green light and the excitation migration time. However, the adaptive change does not result in a significant drop in the overall photochemical efficiency of Photosystem II. These results show that LHCII is a robust adaptable system whose spectral properties can be tuned to the environment for optimal light harvesting.


Assuntos
Clorófitas/metabolismo , Transferência de Energia , Complexos de Proteínas Captadores de Luz/metabolismo , Dicroísmo Circular , Espectrometria de Fluorescência , Temperatura , Fatores de Tempo
12.
Nat Commun ; 11(1): 1460, 2020 03 19.
Artigo em Inglês | MEDLINE | ID: mdl-32193383

RESUMO

Since the discovery of quantum beats in the two-dimensional electronic spectra of photosynthetic pigment-protein complexes over a decade ago, the origin and mechanistic function of these beats in photosynthetic light-harvesting has been extensively debated. The current consensus is that these long-lived oscillatory features likely result from electronic-vibrational mixing, however, it remains uncertain if such mixing significantly influences energy transport. Here, we examine the interplay between the electronic and nuclear degrees of freedom (DoF) during the excitation energy transfer (EET) dynamics of light-harvesting complex II (LHCII) with two-dimensional electronic-vibrational spectroscopy. Particularly, we show the involvement of the nuclear DoF during EET through the participation of higher-lying vibronic chlorophyll states and assign observed oscillatory features to specific EET pathways, demonstrating a significant step in mapping evolution from energy to physical space. These frequencies correspond to known vibrational modes of chlorophyll, suggesting that electronic-vibrational mixing facilitates rapid EET over moderately size energy gaps.


Assuntos
Transferência de Energia , Complexos de Proteínas Captadores de Luz/química , Teoria Quântica , Elétrons , Complexos de Proteínas Captadores de Luz/metabolismo , Modelos Químicos , Folhas de Planta/citologia , Análise Espectral , Tilacoides/metabolismo
13.
Nat Commun ; 11(1): 1295, 2020 03 10.
Artigo em Inglês | MEDLINE | ID: mdl-32157079

RESUMO

Plants prevent photodamage under high light by dissipating excess energy as heat. Conformational changes of the photosynthetic antenna complexes activate dissipation by leveraging the sensitivity of the photophysics to the protein structure. The mechanisms of dissipation remain debated, largely due to two challenges. First, because of the ultrafast timescales and large energy gaps involved, measurements lacked the temporal or spectral requirements. Second, experiments have been performed in detergent, which can induce non-native conformations, or in vivo, where contributions from homologous antenna complexes cannot be disentangled. Here, we overcome both challenges by applying ultrabroadband two-dimensional electronic spectroscopy to the principal antenna complex, LHCII, in a near-native membrane. Our data provide evidence that the membrane enhances two dissipative pathways, one of which is a previously uncharacterized chlorophyll-to-carotenoid energy transfer. Our results highlight the sensitivity of the photophysics to local environment, which may control the balance between light harvesting and dissipation in vivo.


Assuntos
Carotenoides/metabolismo , Membrana Celular/metabolismo , Clorofila/metabolismo , Transferência de Energia , Complexos de Proteínas Captadores de Luz/metabolismo , Nanoestruturas/química , Complexos de Proteínas Captadores de Luz/química , Conformação Proteica
14.
Science ; 367(6482): 1091-1097, 2020 03 06.
Artigo em Inglês | MEDLINE | ID: mdl-32139536

RESUMO

Many disease pathologies can be understood through the elucidation of localized biomolecular networks, or microenvironments. To this end, enzymatic proximity labeling platforms are broadly applied for mapping the wider spatial relationships in subcellular architectures. However, technologies that can map microenvironments with higher precision have long been sought. Here, we describe a microenvironment-mapping platform that exploits photocatalytic carbene generation to selectively identify protein-protein interactions on cell membranes, an approach we term MicroMap (µMap). By using a photocatalyst-antibody conjugate to spatially localize carbene generation, we demonstrate selective labeling of antibody binding targets and their microenvironment protein neighbors. This technique identified the constituent proteins of the programmed-death ligand 1 (PD-L1) microenvironment in live lymphocytes and selectively labeled within an immunosynaptic junction.


Assuntos
Antígeno B7-H1/metabolismo , Membrana Celular/metabolismo , Microambiente Celular , Linfócitos/metabolismo , Mapeamento de Interação de Proteínas/métodos , Mapas de Interação de Proteínas , Catálise , Membrana Celular/efeitos da radiação , Transferência de Energia , Humanos , Células Jurkat , Linfócitos/efeitos da radiação , Metano/análogos & derivados , Metano/química , Metano/efeitos da radiação , Processos Fotoquímicos , Raios Ultravioleta
15.
Phys Med Biol ; 65(12): 125010, 2020 06 17.
Artigo em Inglês | MEDLINE | ID: mdl-32187594

RESUMO

We calculate differential and integrated cross sections for the Compton interaction as well as mass attenuation ([Formula: see text]), mass energy-transfer ([Formula: see text]), and mass energy-absorption ([Formula: see text]) coefficients, within the relativistic impulse approximation (RIA) using Compton profiles (CPs) obtained from unrestricted Hartree-Fock electron densities. We investigate the impact of using molecular as opposed to atomic CPs on dosimetric photon interaction coefficients for air, water and graphite, and compare our cross sections to the simpler Waller-Hartree (WH) and Klein-Nishina (KN) formalisms. We find that differences in [Formula: see text] and [Formula: see text] resulting from the choice of CPs within the RIA are small relative to the differences between the RIA, WH, and KN calculations. Surprisingly, although the WH binding corrections seem accurate when considering [Formula: see text], there are significant discrepancies between the WH and RIA results when we look at [Formula: see text]. The WH theory can differ substantially from the predictions of KN and the RIA in the tens of keV range (e.g. 6%-10% at 20 keV), when Compton scattering becomes the dominant interaction mechanism. For lower energies, the disagreement further grows to about one order of magnitude at 1 keV. However, since the photoelectric effect transfers more energy than the Compton interaction in the tens of keV range and below, the differences in the total [Formula: see text] values resulting from the choice of Compton models (KN, WH, or RIA) are not larger than 0.4%, and the differences between WH and the other two theories are no longer prominent.


Assuntos
Fótons , Radiometria , Espalhamento de Radiação , Ar , Transferência de Energia , Grafite , Água
16.
Proc Natl Acad Sci U S A ; 117(12): 6502-6508, 2020 03 24.
Artigo em Inglês | MEDLINE | ID: mdl-32139606

RESUMO

Carotenoids play a number of important roles in photosynthesis, primarily providing light-harvesting and photoprotective energy dissipation functions within pigment-protein complexes. The carbon-carbon double bond (C=C) conjugation length of carotenoids (N), generally between 9 and 15, determines the carotenoid-to-(bacterio)chlorophyll [(B)Chl] energy transfer efficiency. Here we purified and spectroscopically characterized light-harvesting complex 2 (LH2) from Rhodobacter sphaeroides containing the N = 7 carotenoid zeta (ζ)-carotene, not previously incorporated within a natural antenna complex. Transient absorption and time-resolved fluorescence show that, relative to the lifetime of the S1 state of ζ-carotene in solvent, the lifetime decreases ∼250-fold when ζ-carotene is incorporated within LH2, due to transfer of excitation energy to the B800 and B850 BChls a These measurements show that energy transfer proceeds with an efficiency of ∼100%, primarily via the S1 → Qx route because the S1 → S0 fluorescence emission of ζ-carotene overlaps almost perfectly with the Qx absorption band of the BChls. However, transient absorption measurements performed on microsecond timescales reveal that, unlike the native N ≥ 9 carotenoids normally utilized in light-harvesting complexes, ζ-carotene does not quench excited triplet states of BChl a, likely due to elevation of the ζ-carotene triplet energy state above that of BChl a These findings provide insights into the coevolution of photosynthetic pigments and pigment-protein complexes. We propose that the N ≥ 9 carotenoids found in light-harvesting antenna complexes represent a vital compromise that retains an acceptable level of energy transfer from carotenoids to (B)Chls while allowing acquisition of a new, essential function, namely, photoprotective quenching of harmful (B)Chl triplets.


Assuntos
Proteínas de Bactérias/metabolismo , Bacterioclorofilas/metabolismo , Carotenoides/metabolismo , Complexos de Proteínas Captadores de Luz/metabolismo , Proteínas de Bactérias/química , Carotenoides/química , Transferência de Energia , Cinética , Complexos de Proteínas Captadores de Luz/química , Fotossíntese , Rhodobacter sphaeroides/química , Rhodobacter sphaeroides/metabolismo
17.
J Phys Chem Lett ; 11(5): 1636-1643, 2020 Mar 05.
Artigo em Inglês | MEDLINE | ID: mdl-32013435

RESUMO

High efficiency of light harvesting in photosynthetic pigment-protein complexes is governed by evolutionary-perfected protein-assisted tuning of individual pigment properties and interpigment interactions. Due to the large number of spectrally overlapping pigments in a typical photosynthetic complex, experimental methods often fail to unambiguously identify individual chromophore properties. Here, we report a first-principles-based modeling protocol capable of predicting properties of pigments in protein environment to a high precision. The technique was applied to successfully uncover electronic properties of the Fenna-Matthews-Olson (FMO) pigment-protein complex. Each of the three subunits of the FMO complex contains eight strongly coupled bacteriochlorophyll a (BChl a) pigments. The excitonic structure of FMO can be described by an electronic Hamiltonian containing excitation (site) energies of BChl a pigments and electronic couplings between them. Several such Hamiltonians have been developed in the past based on the information from various spectroscopic measurements of FMO; however, fine details of the excitonic structure and energy transfer in FMO, especially assignments of short-lived high-energy sites, remain elusive. Utilizing polarizable embedding quantum mechanics/molecular mechanics with the effective fragment potentials, we computed the electronic Hamiltonian of FMO that is in general agreement with previously reported empirical Hamiltonians and quantitatively reproduces experimental absorption and circular dichroism spectra of the FMO protein. The developed computational protocol is sufficiently simple and can be utilized for predictive modeling of other wild-type and mutated photosynthetic pigment-protein complexes.


Assuntos
Proteínas de Bactérias/metabolismo , Complexos de Proteínas Captadores de Luz/metabolismo , Simulação de Dinâmica Molecular , Teoria Quântica , Proteínas de Bactérias/química , Bacterioclorofila A/química , Bacterioclorofila A/metabolismo , Chlorobi/metabolismo , Dicroísmo Circular , Transferência de Energia , Gases/química , Complexos de Proteínas Captadores de Luz/química , Fotossíntese
18.
PLoS One ; 15(2): e0228543, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32045426

RESUMO

Two molecules, 7-(diethylamino)coumarin-3-carbohydrazide (DCCH) and fluorescein-5-thiosemicarbazide (FTSC) were investigated in different solvents, under varying pH conditions regarding their spectroscopic properties for the usage as a Förster Resonance Energy Transfer (FRET) pair to study the molecular interaction between cellulosic surfaces. All the relevant spectroscopic properties to determine the Förster distance were measured and the performance as a FRET system was checked. From the results, it is clear that the environmental conditions need to be accurately controlled as both, but especially the FTSC dyes are sensitive to changes. For high enough concentrations positive FRET systems were observed in DMF, DMSO, H2O, THF and alkaline DMF. However due to the low quantum yield of the unmodified DCCH throughout the investigated parameter range and the strong environmental dependency of FTSC, both dyes are not preferable for being used in a FRET system for studying interaction between cellulosic surfaces.


Assuntos
Cumarínicos/química , Fluoresceínas/química , Transferência Ressonante de Energia de Fluorescência/métodos , Hidrazinas/química , Solventes/química , Análise Espectral/métodos , Transferência de Energia/efeitos dos fármacos , Concentração de Íons de Hidrogênio , Solventes/farmacologia , Espectrometria de Fluorescência/métodos , Espectrofotometria Ultravioleta/métodos
19.
Artigo em Inglês | MEDLINE | ID: mdl-32073347

RESUMO

Sudan III is a coloring agent used in chemical industries and food additives. This article uses spectroscopic and molecular docking methods to investigate the interaction of Sudan III with bovine serum albumin (BSA) under a physiological condition. Spectroscopic analysis of the emission quenching revealed that the quenching mechanism of BSA by Sudan III was static. The binding sites and constants of Sudan III-BSA complex were observed to be from 0.72 and 6.41 × 102 L·mol-1 to 0.69 and 5.83 × 102 L·mol-1 at 298 and 310 K, respectively. The enthalpy change (ΔH) and entropy change (ΔS) revealed that van der Waals forces and hydrogen bonds stabilized the Sudan III-BSA complex. Energy transfer from tryptophan to Sudan III occurred by a fluorescence resonance energy transfer mechanism, and the r distance (3.32 nm) had been determined. The results of UV-Vis absorption, synchronous, three-dimensional fluorescence, and circular dichroism spectra showed that Sudan III induced conformational changes of BSA. Molecular docking studies revealed that Sudan III situated within subdomain IIA of BSA. A study on the interaction between Sudan III and BSA was of fundamental importance for providing more information about the potential toxicological effect of chemicals at the molecular level.


Assuntos
Compostos Azo/química , Corantes de Alimentos/química , Soroalbumina Bovina/química , Animais , Sítios de Ligação , Dicroísmo Circular , Transferência de Energia , Simulação de Acoplamento Molecular , Ligação Proteica , Espectrometria de Fluorescência , Espectrofotometria Ultravioleta , Termodinâmica
20.
J Chem Phys ; 152(4): 045103, 2020 Jan 31.
Artigo em Inglês | MEDLINE | ID: mdl-32007039

RESUMO

Recent time-resolved experiments and accompanying molecular dynamics simulations allow us to monitor the flow of vibrational energy in biomolecules. As a simple means to describe these experimental and simulated data, Buchenberg et al. [J. Phys. Chem. Lett. 7, 25 (2016)] suggested a master equation model that accounts for the energy transport from an initially excited residue to some target residue. The transfer rates of the model were obtained from two scaling rules, which account for the energy transport through the backbone and via tertiary contacts, respectively, and were parameterized using simulation data of a small α-helical protein at low temperatures. To extend the applicability of the model to general proteins at room temperature, here a new parameterization is presented, which is based on extensive nonequilibrium molecular dynamics simulations of a number of model systems. With typical transfer times of 0.5-1 ps between adjacent residues, backbone transport represents the fastest channel of energy flow. It is well described by a diffusive-type scaling rule, which requires only an overall backbone diffusion coefficient and interatom distances as input. Contact transport, e.g., via hydrogen bonds, is considerably slower (6-30 ps) at room temperature. A new scaling rule depending on the inverse square contact distance is suggested, which is shown to successfully describe the energy transport in the allosteric protein PDZ3. Since both scaling rules require only the structure of the considered system, the model provides a simple and general means to predict energy transport in proteins. To identify the pathways of energy transport, Monte Carlo Markov chain simulations are performed, which highlight the competition between backbone and contact transport channels.


Assuntos
Modelos Químicos , Proteínas/química , Transferência de Energia , Modelos Moleculares , Simulação de Dinâmica Molecular , Estrutura Secundária de Proteína , Proteínas/metabolismo
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