Nejvíce citovaný článek - PubMed ID 27509302
A Unified Picture of S* in Carotenoids
Target analysis is employed to resolve the ground and excited state properties from simultaneously measured Femtosecond Stimulated Raman Spectra (FSRS) and Transient Absorption Spectra (TAS). FSRS is a three-pulse technique, involving picosecond Raman pump pulses and femtosecond visible pump and probe pulses. The TAS are needed to precisely estimate the properties of the Instrument Response Function. The prezero "coherent artifact" present during the overlap of the three pulses is described by a damped oscillation with a frequency (ω - ωn) where ωn is a ground state resonance Raman frequency. Simultaneous target analysis of the FSRS and TAS allows the complete excited state dynamics to be resolved with a time resolution better than 100 fs. The model system studied is the carotenoid lycopene in tetrahydrofuran. The lycopene dynamics show a spectral evolution with seven states, including a biphasic cooling process during the S2-S1 internal conversion, multiple S1 lifetimes, and an S* state decaying with a lifetime of 7 ps.
- Publikační typ
- časopisecké články MeSH
Cyanobacteria use large antenna complexes called phycobilisomes (PBSs) for light harvesting. However, intense light triggers non-photochemical quenching, where the orange carotenoid protein (OCP) binds to PBS, dissipating excess energy as heat. The mechanism of efficiently transferring energy from phycocyanobilins in PBS to canthaxanthin in OCP remains insufficiently understood. Using cryo-electron microscopy, we unveiled the OCP-PBS complex structure at 1.6- to 2.1-angstrom resolution, showcasing its inherent flexibility. Using multiscale quantum chemistry, we disclosed the quenching mechanism. Identifying key protein residues, we clarified how canthaxanthin's transition dipole moment in its lowest-energy dark state becomes large enough for efficient energy transfer from phycocyanobilins. Our energy transfer model offers a detailed understanding of the atomic determinants of light harvesting regulation and antenna architecture in cyanobacteria.
The functions of both (bacterio) chlorophylls and carotenoids in light-harvesting complexes have been extensively studied during the past decade, yet, the involvement of BChl a high-energy Soret band in the cascade of light-harvesting processes still remains a relatively unexplored topic. Here, we present transient absorption data recorded after excitation of the Soret band in the LH2 complex from Rhodoblastus acidophilus. Comparison of obtained data to those recorded after excitation of rhodopin glucoside and B800 BChl a suggests that no Soret-to-Car energy transfer pathway is active in LH2 complex. Furthermore, a spectrally rich pattern observed in the spectral region of rhodopin glucoside ground state bleaching (420-550 nm) has been assigned to an electrochromic shift. The results of global fitting analysis demonstrate two more features. A 6 ps component obtained exclusively after excitation of the Soret band has been assigned to the response of rhodopin glucoside to excess energy dissipation in LH2. Another time component, ~ 450 ps, appearing independently of the excitation wavelength was assigned to BChl a-to-Car triplet-triplet transfer. Presented data demonstrate several new features of LH2 complex and its behavior following the excitation of the Soret band.
- Klíčová slova
- Antenna complex, Carotenoids, Electrochromic shift, Energy transfer, Excess energy, LH2,
- MeSH
- bakteriochlorofyly metabolismus MeSH
- Beijerinckiaceae MeSH
- glukosidy MeSH
- karotenoidy * metabolismus MeSH
- světlosběrné proteinové komplexy * metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriochlorofyly MeSH
- glukosidy MeSH
- karotenoidy * MeSH
- rhodopin glucoside MeSH Prohlížeč
- světlosběrné proteinové komplexy * MeSH
Carotenoids are an integral part of natural photosynthetic complexes, with tasks ranging from light harvesting to photoprotection. Their underlying energy deactivation network of optically dark and bright excited states is extremely efficient: after excitation of light with up to 2.5 eV of photon energy, the system relaxes back to ground state on a time scale of a few picoseconds. In this article, we summarize how a model based on the vibrational energy relaxation approach (VERA) explains the main characteristics of relaxation dynamics after one-photon excitation with special emphasis on the so-called S* state. Lineshapes after two-photon excitation are beyond the current model of VERA. We outline this future line of research in our article. In terms of experimental method development, we discuss which techniques are needed to better describe energy dissipation effects in carotenoids and within the first solvation shell.
- MeSH
- fotony MeSH
- fotosyntetická reakční centra (proteinové komplexy) * MeSH
- karotenoidy * MeSH
- světlosběrné proteinové komplexy MeSH
- vibrace MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
- Názvy látek
- fotosyntetická reakční centra (proteinové komplexy) * MeSH
- karotenoidy * MeSH
- světlosběrné proteinové komplexy MeSH
Here, we propose a possible photoactivation mechanism of a 35-kDa blue light-triggered photoreceptor, the Orange Carotenoid Protein (OCP), suggesting that the reaction involves the transient formation of a protonated ketocarotenoid (oxocarbenium cation) state. Taking advantage of engineering an OCP variant carrying the Y201W mutation, which shows superior spectroscopic and structural properties, it is shown that the presence of Trp201 augments the impact of one critical H-bond between the ketocarotenoid and the protein. This confers an unprecedented homogeneity of the dark-adapted OCP state and substantially increases the yield of the excited photoproduct S*, which is important for the productive photocycle to proceed. A 1.37 Å crystal structure of OCP Y201W combined with femtosecond time-resolved absorption spectroscopy, kinetic analysis, and deconvolution of the spectral intermediates, as well as extensive quantum chemical calculations incorporating the effect of the local electric field, highlighted the role of charge-transfer states during OCP photoconversion.
- MeSH
- bakteriální proteiny chemie metabolismus MeSH
- fotochemie * MeSH
- karotenoidy metabolismus MeSH
- kinetika MeSH
- konformace proteinů MeSH
- krystalografie MeSH
- molekulární modely MeSH
- vodíková vazba MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- karotenoidy MeSH
- orange carotenoid protein, Synechocystis MeSH Prohlížeč
The major light-harvesting complex of photosystem II (LHCII) is the main contributor to sunlight energy harvesting in plants. The flexible design of LHCII underlies a photoprotective mechanism whereby this complex switches to a dissipative state in response to high light stress, allowing the rapid dissipation of excess excitation energy (non-photochemical quenching, NPQ). In this work, we locked single LHCII trimers in a quenched conformation after immobilization of the complexes in polyacrylamide gels to impede protein interactions. A comparison of their pigment excited-state dynamics with quenched LHCII aggregates in buffer revealed the presence of a new spectral band at 515 nm arising after chlorophyll excitation. This is suggested to be the signature of a carotenoid excited state, linked to the quenching of chlorophyll singlet excited states. Our data highlight the marked sensitivity of pigment excited-state dynamics in LHCII to structural changes induced by the environment.
- Klíčová slova
- Molecular Structure, Optical Property, Physical Optics,
- Publikační typ
- časopisecké články MeSH
In some molecular systems, such as nucleobases, polyenes or the active ingredients of sunscreens, substantial amounts of photo-excitation energy are dissipated on a sub-picosecond time scale, raising questions such as: where does this energy go or among which degrees of freedom it is being distributed at such early times? Here we use transient absorption spectroscopy to track excitation energy dispersing from the optically accessible vibronic subsystem into the remaining vibrational subsystem of the solute and solvent. Monitoring the flow of energy during vibrational redistribution enables quantification of local molecular heating. Subsequent heat dissipation away from the solute molecule is characterized by classical thermodynamics and molecular dynamics simulations. Hence, we present a holistic approach that tracks the internal temperature and vibronic distribution from the act of photo-excitation to the restoration of the global equilibrium. Within this framework internal vibrational redistribution and vibrational cooling are emergent phenomena. We demonstrate the validity of the framework by examining a highly controversial example, carotenoids. We show that correctly accounting for the local temperature unambiguously explains their energetically and temporally congested spectral dynamics without the ad hoc postulation of additional 'dark' states. An immediate further application of this approach would be to monitor the excitation and thermal dynamics of pigment-protein systems.
- Publikační typ
- časopisecké články MeSH
The peripheral light-harvesting antenna complex (LH2) of purple photosynthetic bacteria is an ideal testing ground for models of structure-function relationships due to its well-determined molecular structure and ultrafast energy deactivation. It has been the target for numerous studies in both theory and ultrafast spectroscopy; nevertheless, certain aspects of the convoluted relaxation network of LH2 lack a satisfactory explanation by conventional theories. For example, the initial carotenoid-to-bacteriochlorophyll energy transfer step necessary on visible light excitation was long considered to follow the Förster mechanism, even though transfer times as short as 40 femtoseconds (fs) have been observed. Such transfer times are hard to accommodate by Förster theory, as the moderate coupling strengths found in LH2 suggest much slower transfer within this framework. In this study, we investigate LH2 from Phaeospirillum (Ph.) molischianum in two types of transient absorption experiments-with narrowband pump and white-light probe resulting in 100 fs time resolution, and with degenerate broadband 10 fs pump and probe pulses. With regard to the split Qx band in this system, we show that vibronically mediated transfer explains both the ultrafast carotenoid-to-B850 transfer, and the almost complete lack of transfer to B800. These results are beyond Förster theory, which predicts an almost equal partition between the two channels.
- Klíčová slova
- Excitation energy transfer, Excitons, LH2, Photosynthesis, Ultrafast spectroscopy,
- MeSH
- bakteriochlorofyly metabolismus MeSH
- časové faktory MeSH
- Fourierova analýza MeSH
- karotenoidy metabolismus MeSH
- lasery MeSH
- přenos energie * MeSH
- Proteobacteria metabolismus MeSH
- spektrofotometrie ultrafialová MeSH
- světlosběrné proteinové komplexy metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriochlorofyly MeSH
- karotenoidy MeSH
- světlosběrné proteinové komplexy MeSH
