Photophysics of plasmonically enhanced self-assembled artificial light-harvesting nanoantennas.

The design of efficient artificial light-harvesting antennas is essential for enabling the widespread use of solar energy. Natural photosynthetic systems offer valuable inspiration, but many rely on complex pigment-protein interactions and have limited spectral coverage, which pose challenges for rational design. Chlorosome mimics, which are self-assembling pigment aggregates inspired by green photosynthetic bacteria, offer structural simplicity, flexible tunability, and strong excitonic coupling through pigment-pigment interactions.

Direct Synthesis and Characterization of Hydrophilic Cu-Deficient Copper Indium Sulfide Quantum Dots.

Copper indium sulfide (CIS) nanocrystals constitute a promising alternative to cadmium- and lead-containing nanoparticles. We report a synthetic method that yields hydrophilic, core-only CIS quantum dots, exhibiting size-dependent, copper-deficient composition and optical properties that are suitable for direct coupling to biomolecules and nonradiative energy transfer applications. To assist such applications, we complemented previous studies covering the femtosecond-picosecond time scale with the investigation of slower radiative and nonradiative processes on the nanosecond time scale, using both time-resolved emission and transient absorption.

Understanding delayed fluorescence and triplet decays of Protoporphyrin IX under hypoxic conditions.

Photosensitizers of singlet oxygen exhibit three main types of reverse intersystem-crossing (RISC): thermally activated, triplet-triplet annihilation, and singlet oxygen feedback. RISC can be followed by delayed fluorescence (DF) emission, which can provide important information about the excited state dynamics in the studied system. An excellent model example is a widely used clinical photosensitizer Protoporphyrin IX, which manifests all three mentioned types of RISC and DF.

Superradiance of bacteriochlorophyll c aggregates in chlorosomes of green photosynthetic bacteria.

Chlorosomes are the main light-harvesting complexes of green photosynthetic bacteria that are adapted to a phototrophic life at low-light conditions. They contain a large number of bacteriochlorophyll c, d, or e molecules organized in self-assembling aggregates. Tight packing of the pigments results in strong excitonic interactions between the monomers, which leads to a redshift of the absorption spectra and excitation delocalization.

Photoprotection of Photosynthetic Pigments in Plant One-Helix Protein 1/2 Heterodimers.

One-helix proteins 1 and 2 (OHP1/2) are members of the family of light-harvesting-like proteins (LIL) in plants, and their potential function(s) have been initially analyzed only recently. OHP1 and OHP2 are structurally related to the transmembrane α-helices 1 and 3 of all members of the light-harvesting complex (LHC) superfamily. OHPs form heterodimers which bind 6 chlorophylls (Chls) and two carotenoids .

Temperature Dependence of Chlorophyll Triplet Quenching in Two Photosynthetic Light-Harvesting Complexes from Higher Plants and Dinoflagellates.

Chlorophyll (Chl) triplet states generated in photosynthetic light-harvesting complexes (LHCs) can be quenched by carotenoids to prevent the formation of reactive singlet oxygen. Although this quenching occurs with an efficiency close to 100% at physiological temperatures, the Chl triplets are often observed at low temperatures. This might be due to the intrinsic temperature dependence of the Dexter mechanism of excitation energy transfer, which governs triplet quenching, or by temperature-induced conformational changes.

Quenching of chlorophyll triplet states by carotenoids in algal light-harvesting complexes related to fucoxanthin-chlorophyll protein.

We have used time-resolved absorption and fluorescence spectroscopy with nanosecond resolution to study triplet energy transfer from chlorophylls to carotenoids in a protective process that prevents the formation of reactive singlet oxygen. The light-harvesting complexes studied were isolated from Chromera velia, belonging to a group Alveolata, and Xanthonema debile and Nannochloropsis oceanica, both from Stramenopiles. All three light-harvesting complexes are related to fucoxanthin-chlorophyll protein, but contain only chlorophyll a and no chlorophyll c.

In situ mapping of the energy flow through the entire photosynthetic apparatus.

Absorption of sunlight is the first step in photosynthesis, which provides energy for the vast majority of organisms on Earth. The primary processes of photosynthesis have been studied extensively in isolated light-harvesting complexes and reaction centres, however, to understand fully the way in which organisms capture light it is crucial to also reveal the functional relationships between the individual complexes. Here we report the use of two-dimensional electronic spectroscopy to track directly the excitation-energy flow through the entire photosynthetic system of green sulfur bacteria.

Triplet-triplet energy transfer from chlorophylls to carotenoids in two antenna complexes from dinoflagellate Amphidinium carterae.

Room temperature transient absorption spectroscopy with nanosecond resolution was used to study quenching of the chlorophyll triplet states by carotenoids in two light-harvesting complexes of the dinoflagellate Amphidinium carterae: the water soluble peridinin-chlorophyll protein complex and intrinsic, membrane chlorophyll a-chlorophyll c2-peridinin protein complex. The combined study of the two complexes facilitated interpretation of a rather complicated relaxation observed in the intrinsic complex. While a single carotenoid triplet state was resolved in the peridinin-chlorophyll protein complex, evidence of at least two different carotenoid triplets was obtained for the intrinsic light-harvesting complex.

Energy transfer in aggregates of bacteriochlorophyll c self-assembled with azulene derivatives.

Bacteriochlorophyll (BChl) c is the main light-harvesting pigment of certain photosynthetic bacteria. It is found in the form of self-assembled aggregates in the so-called chlorosomes. Here we report the results of co-aggregation experiments of BChl c with azulene and its tailored derivatives.

2D Electronic Spectroscopy Reveals Excitonic Structure in the Baseplate of a Chlorosome.

In green photosynthetic bacteria, the chlorosome baseplate mediates excitation energy transfer from the interior of the light-harvesting chlorosome toward the reaction centers. However, the electronic states of the baseplate remain unexplored, hindering the mechanistic understanding of the baseplate as an excitation energy collector and mediator. Here we use two-dimensional spectroscopy to study the excited state structure and internal energy relaxation in the baseplate of green sulfur bacterium Chlorobaculum tepidum.

Unraveling the nature of coherent beatings in chlorosomes.

Coherent two-dimensional (2D) spectroscopy at 80 K was used to study chlorosomes isolated from green sulfur bacterium Chlorobaculum tepidum. Two distinct processes in the evolution of the 2D spectrum are observed. The first being exciton diffusion, seen in the change of the spectral shape occurring on a 100-fs timescale, and the second being vibrational coherences, realized through coherent beatings with frequencies of 91 and 145 cm(-1) that are dephased during the first 1.

Structural and functional roles of carotenoids in chlorosomes.

Chlorosomes are large light-harvesting complexes found in three phyla of anoxygenic photosynthetic bacteria. Chlorosomes are primarily composed of self-assembling pigment aggregates. In addition to the main pigment, bacteriochlorophyll c, d, or e, chlorosomes also contain variable amounts of carotenoids.

Two-dimensional electronic spectroscopy reveals ultrafast energy diffusion in chlorosomes.

Chlorosomes are light-harvesting antennae that enable exceptionally efficient light energy capture and excitation transfer. They are found in certain photosynthetic bacteria, some of which live in extremely low-light environments. In this work, chlorosomes from the green sulfur bacterium Chlorobaculum tepidum were studied by coherent electronic two-dimensional (2D) spectroscopy.

The lamellar spacing in self-assembling bacteriochlorophyll aggregates is proportional to the length of the esterifying alcohol.

Chlorosomes from green photosynthetic bacteria are large photosynthetic antennae containing self-assembling aggregates of bacteriochlorophyll c, d, or e. The pigments within chlorosomes are organized in curved lamellar structures. Aggregates with similar optical properties can be prepared in vitro, both in polar as well as non-polar solvents.

Excited state properties of aryl carotenoids.

Excited-state properties of aryl carotenoids, important components of light harvesting antennae of green sulfur bacteria, have been studied by femtosecond transient absorption spectroscopy. To explore effects of the conjugated aryl group, we have studied a series of aryl carotenoids with conjugated phi-ring, chlorobactene, beta-isorenieratene and isorenieratene, and compared them with their non-aryl counterparts gamma-carotene and beta-carotene, which contain beta-ring. Changing beta-ring to phi-ring did not reveal any changes in absorption spectra, indicating negligible effect of the phi-ring on the effective conjugation length.

Structure of chlorosomes from the green filamentous bacterium Chloroflexus aurantiacus.

The green filamentous bacterium Chloroflexus aurantiacus employs chlorosomes as photosynthetic antennae. Chlorosomes contain bacteriochlorophyll aggregates and are attached to the inner side of a plasma membrane via a protein baseplate. The structure of chlorosomes from C.

The length of esterifying alcohol affects the aggregation properties of chlorosomal bacteriochlorophylls.

Chlorosomes, the main light-harvesting complexes of green photosynthetic bacteria, contain bacteriochlorophyll (BChl) molecules in the form of self-assembling aggregates. To study the role of esterifying alcohols in BChl aggregation we have prepared a series of bacteriochlorophyllide c (BChlide c) derivatives differing in the length of the esterifying alcohol (C(1), C(4), C(8) and C(12)). Their aggregation behavior was studied both in polar (aqueous buffer) and nonpolar (hexane) environments and the esterifying alcohols were found to play an essential role.

Hexanol-induced order-disorder transitions in lamellar self-assembling aggregates of bacteriochlorophyll c in Chlorobium tepidum chlorosomes.

Chlorosomes are light-harvesting complexes of green photosynthetic bacteria. Chlorosomes contain bacteriochlorophyll (BChl) c, d, or e aggregates that exhibit strong excitonic coupling. The short-range order, which is responsible for the coupling, has been proposed to be augmented by pigment arrangement into undulated lamellar structures with spacing between 2 and 3 nm.

Effect of quinones on formation and properties of bacteriochlorophyll c aggregates.

Chlorosomes of green photosynthetic bacterium Chlorobium tepidum contain aggregates of bacteriochlorophyll c (BChl c) with carotenoids and isoprenoid quinones. BChl aggregates with very similar optical properties can be prepared also in vitro either in non-polar solvents or in aqueous buffers with addition of lipids and/or carotenoids. In this work, we show that the aggregation of BChl c in aqueous buffer can be induced also by quinones (vitamin K(1 )and K(2)), provided they are non-polar due to a hydrophobic side-chain.

Internal structure of chlorosomes from brown-colored chlorobium species and the role of carotenoids in their assembly.

Chlorosomes are the main light harvesting complexes of green photosynthetic bacteria. Recently, a lamellar model was proposed for the arrangement of pigment aggregates in Chlorobium tepidum chlorosomes, which contain bacteriochlorophyll (BChl) c as the main pigment. Here we demonstrate that the lamellar organization is also found in chlorosomes from two brown-colored species (Chl.

Excitation energy transfer in chlorosomes of Chlorobium phaeobacteroides strain CL1401: the role of carotenoids.

The role of carotenoids in chlorosomes of the green sulfur bacterium Chlorobium phaeobacteroides, containing bacteriochlorophyll (BChl) e and the carotenoid (Car) isorenieratene as main pigments, was studied by steady-state fluorescence excitation, picosecond single-photon timing and femtosecond transient absorption (TA) spectroscopy. In order to obtain information about energy transfer from Cars in this photosynthetic light-harvesting antenna with high spectral overlap between Cars and BChls, Car-depleted chlorosomes, obtained by inhibition of Car biosynthesis by 2-hydroxybiphenyl, were employed in a comparative study with control chlorosomes. Excitation spectra measured at room temperature give an efficiency of 60-70% for the excitation energy transfer from Cars to BChls in control chlorosomes.