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. However, these pigment aggregates suffer from limited absorption in the green and near-infrared regions and, similarly to other light-harvesting systems, reduced energy transfer efficiency at high donor concentrations. One promising strategy to overcome these limitations is the integration of plasmonic nanoparticles, which enhance local electromagnetic fields, increase spectral coverage, and make new energetic pathways accessible. Although plasmonic enhancement has been widely studied in pigment-protein complexes like Photosystem I and light-harvesting complexes (LHCs), its application to pigment-pigment self-assembled systems remains largely unexplored. This perspective presents recent advances in biomimetic light-harvesting design with chlorosome mimics and explores the potential for plasmonic enhancement of photophysics in these systems. We examine the structure of chlorosomes and their artificial mimics to understand the role of pigment-pigment interactions in facilitating highly efficient energy transfer.

• Publication type
• Journal Article MeSH
• Review MeSH

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. Due to the large amount of disorder present in chlorosomes, the extent of delocalization is limited and further decreases in time after excitation. In this work we address the question whether the excitonic interactions between the bacteriochlorophyll c molecules are strong enough to maintain some extent of delocalization even after exciton relaxation. That would manifest itself by collective spontaneous emission, so-called superradiance. We show that despite a very low fluorescence quantum yield and short excited state lifetime, both caused by the aggregation, chlorosomes indeed exhibit superradiance. The emission occurs from states delocalized over at least two molecules. In other words, the dipole strength of the emissive states is larger than for a bacteriochlorophyll c monomer. This represents an important functional mechanism increasing the probability of excitation energy transfer that is vital at low-light conditions. Similar behaviour was observed also in one type of artificial aggregates, and this may be beneficial for their potential use in artificial photosynthesis.

• MeSH
• Bacteria metabolism   MeSH
• Bacterial Proteins metabolism   MeSH
• Bacteriochlorophylls metabolism   MeSH
• Pigments, Biological metabolism   MeSH
• Photosynthesis * MeSH
• Energy Transfer MeSH
• Protein Aggregates * MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• bacteriochlorophyll c MeSH Browser
• Bacterial Proteins MeSH
• Bacteriochlorophylls MeSH
• Pigments, Biological MeSH
• Protein Aggregates * MeSH

Chlorosomes from green photosynthetic bacteria belong to the most effective light-harvesting antennas found in nature. Quinones incorporated in bacterichlorophyll (BChl) c aggregates inside chlorosomes play an important redox-dependent photo-protection role against oxidative damage of bacterial reaction centers. Artificial BChl c aggregates with and without quinones were prepared. We applied hole-burning spectroscopy and steady-state absorption and emission techniques at 1.9 K and two different redox potentials to investigate the role of quinones and redox potential on BChl c aggregates at low temperatures. We show that quinones quench the excitation energy in a similar manner as at room temperature, yet the quenching process is not as efficient as for chlorosomes. Interestingly, our data suggest that excitation quenching partially proceeds from higher excitonic states competing with ultrafast exciton relaxation. Moreover, we obtained structure-related parameters such as reorganization energies and inhomogeneous broadening of the lowest excited state, providing experimental ground for theoretical studies aiming at designing plausible large-scale model for BChl c aggregates including disorder.

• MeSH
• Absorption MeSH
• Bacterial Proteins analysis   chemistry   MeSH
• Bacteriochlorophylls analysis   chemistry   MeSH
• Fluorescence MeSH
• Oxidation-Reduction MeSH
• Spectrum Analysis methods   MeSH
• Temperature MeSH
• Vitamin K 2 chemistry   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• bacteriochlorophyll c MeSH Browser
• Bacterial Proteins MeSH
• Bacteriochlorophylls MeSH
• Vitamin K 2 MeSH

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. Here, we use X-ray scattering and electron cryomicroscopy, complemented with absorption spectroscopy and pigment analysis, to compare the morphologies, structures, and pigment compositions of chlorosomes from Chloroflexus aurantiacus grown under two different light conditions and Chlorobaculum tepidum. High-purity chlorosomes from C. aurantiacus contain about 20% more carotenoid per bacteriochlorophyll c molecule when grown under low light than when grown under high light. This accentuates the light-harvesting function of carotenoids, in addition to their photoprotective role. The low-light chlorosomes are thicker due to the overall greater content of pigments and contain domains of lamellar aggregates. Experiments where carotenoids were selectively extracted from intact chlorosomes using hexane proved that they are located in the interlamellar space, as observed previously for species belonging to the phylum Chlorobi. A fraction of the carotenoids are localized in the baseplate, where they are bound differently and cannot be removed by hexane. In C. tepidum, carotenoids cannot be extracted by hexane even from the chlorosome interior. The chemical structure of the pigments in C. tepidum may lead to π-π interactions between carotenoids and bacteriochlorophylls, preventing carotenoid extraction. The results provide information about the nature of interactions between bacteriochlorophylls and carotenoids in the protein-free environment of the chlorosome interior.

• MeSH
• Bacterial Chromatophores MeSH
• Pigments, Biological MeSH
• Chloroflexus cytology   metabolism   MeSH
• X-Ray Diffraction MeSH
• Phycobiliproteins chemistry   physiology   MeSH
• Carotenoids chemistry   metabolism   MeSH
• Molecular Structure MeSH
• Organelles physiology   MeSH
• Light * MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Research Support, U.S. Gov't, Non-P.H.S. MeSH
• Names of Substances
• Pigments, Biological MeSH
• Phycobiliproteins MeSH
• Carotenoids MeSH

Chlorosomes, the light-harvesting antennae of green photosynthetic bacteria, are based on large aggregates of bacteriochlorophyll molecules. Aggregates with similar properties to those in chlorosomes can also be prepared in vitro. Several agents were shown to induce aggregation of bacteriochlorophyll c in aqueous environments, including certain lipids, carotenes, and quinones. A key distinguishing feature of bacteriochlorophyll c aggregates, both in vitro and in chlorosomes, is a large (>60 nm) red shift of their Q(y) absorption band compared with that of the monomers. In this study, we investigate the self-assembly of bacteriochlorophyll c with the xanthophyll astaxanthin, which leads to the formation of a new type of complexes. Our results indicate that, due to its specific structure, astaxanthin molecules competes with bacteriochlorophylls for the bonds involved in the aggregation, thus preventing the formation of any significant red shift compared with pure bacteriochlorophyll c in aqueous buffer. A strong interaction between both the types of pigments in the developed assemblies, is manifested by a rather efficient (~40%) excitation energy transfer from astaxanthin to bacteriochlorophyll c, as revealed by fluorescence excitation spectroscopy. Results of transient absorption spectroscopy show that the energy transfer is very fast (<500 fs) and proceeds through the S(2) state of astaxanthin.

• MeSH
• Bacterial Proteins chemistry   isolation & purification   metabolism   MeSH
• Bacteriochlorophylls chemistry   isolation & purification   metabolism   MeSH
• Chlorobium chemistry   MeSH
• Photosynthesis MeSH
• Energy Transfer * MeSH
• Spectrum Analysis MeSH
• Light MeSH
• Light-Harvesting Protein Complexes chemistry   metabolism   MeSH
• Xanthophylls chemistry   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• astaxanthine MeSH Browser
• bacteriochlorophyll c MeSH Browser
• Bacterial Proteins MeSH
• Bacteriochlorophylls MeSH
• Light-Harvesting Protein Complexes MeSH
• Xanthophylls MeSH

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. In order to gain insight into their structure we examined hexane-induced aggregates of purified bacteriochlorophyll c by X-ray scattering. The bacteriochlorophyll c aggregates exhibit scattering features that are virtually identical to those of native chlorosomes demonstrating that the self-assembly of these pigments is fully encoded in their chemical structure. Thus, the hexane-induced aggregates constitute an excellent model to study the effects of chemical structure on assembly. Using bacteriochlorophyllides transesterified with different alcohols we have established a linear relationship between the esterifying alcohol length and the lamellar spacing. The results provide a structural basis for lamellar spacing variability observed for native chlorosomes from different species. A plausible physiological role of this variability is discussed. The X-ray scattering also confirmed the assignments of peaks, which arise from the crystalline baseplate in the native chlorosomes.

• MeSH
• Alcohols chemistry   MeSH
• Anisotropy MeSH
• Bacteriochlorophylls chemistry   metabolism   MeSH
• Cellular Structures metabolism   MeSH
• Chlorobium metabolism   MeSH
• Esterification MeSH
• Hexanes chemistry   MeSH
• Protein Structure, Quaternary MeSH
• Scattering, Radiation MeSH
• X-Rays MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Alcohols MeSH
• Bacteriochlorophylls MeSH
• Hexanes MeSH

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. aurantiacus was investigated by using a combination of cryo-electron microscopy and X-ray diffraction and compared with that of Chlorobi species. Cryo-electron tomography revealed thin chlorosomes for which a distinct crystalline baseplate lattice was visualized in high-resolution projections. The baseplate is present only on one side of the chlorosome, and the lattice dimensions suggest that a dimer of the CsmA protein is the building block. The bacteriochlorophyll aggregates inside the chlorosome are arranged in lamellae, but the spacing is much greater than that in Chlorobi species. A comparison of chlorosomes from different species suggested that the lamellar spacing is proportional to the chain length of the esterifying alcohols. C. aurantiacus chlorosomes accumulate larger quantities of carotenoids under high-light conditions, presumably to provide photoprotection. The wider lamellae allow accommodation of the additional carotenoids and lead to increased disorder within the lamellae.

• MeSH
• Bacterial Chromatophores MeSH
• Bacteriochlorophylls physiology   MeSH
• Cell Membrane MeSH
• Chloroflexus metabolism   MeSH
• X-Ray Diffraction MeSH
• Intracellular Membranes MeSH
• Organelles physiology   ultrastructure   MeSH
• Light-Harvesting Protein Complexes physiology   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Research Support, U.S. Gov't, Non-P.H.S. MeSH
• Names of Substances
• Bacteriochlorophylls MeSH
• Light-Harvesting Protein Complexes MeSH

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. Polar vitamin K(3, )which possess the same functional group as K(1 )and K(2), does not induce the aggregation. The results confirm a principal role of the hydrophobic interactions as a driving force for the aggregation of chlorosomal BChls. The chlorosomal quinones play an important role in a redox-dependent excitation quenching, which may protect the cells against damage under oxygenic conditions. We found that aggregates of BChl c with vitamin K(1 )and K(2) exhibit an excitation quenching as well. The amplitude of the quenching depends on quinone concentration, as determined from fluorescence measurements. No lipid is necessary to induce the quenching, which therefore originates mainly from interactions of BChl c with quinones incorporated in the aggregate structure. In contrast, only a weak quenching was observed for dimers of BChl c in buffer (either with or without vitamin K(3)) and also for BChl c aggregates prepared with a lipid (lecithin). Thus, the weak quenching seems to be a property of BChl c itself.

• MeSH
• Bacterial Proteins metabolism   MeSH
• Bacteriochlorophylls metabolism   MeSH
• Quinones metabolism   MeSH
• Chlorobium metabolism   MeSH
• Spectrometry, Fluorescence MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• bacteriochlorophyll c MeSH Browser
• Bacterial Proteins MeSH
• Bacteriochlorophylls MeSH
• Quinones MeSH

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. phaeovibrioides and Chl. phaeobacteroides) containing BChl e as the main pigment. This suggests that the lamellar model is universal among green sulfur bacteria. In contrast to green-colored Chl. tepidum, chlorosomes from the brown-colored species often contain domains of lamellar aggregates that may help them to survive in extremely low light conditions. We suggest that carotenoids are localized between the lamellar planes and drive lamellar assembly by augmenting hydrophobic interactions. A model for chlorosome assembly, which accounts for the role of carotenoids and secondary BChl homologs, is presented.

• MeSH
• Bacteriochlorophylls chemistry   metabolism   MeSH
• Models, Biological MeSH
• Models, Chemical * MeSH
• Chlorobium chemistry   metabolism   ultrastructure   MeSH
• Carotenoids chemistry   metabolism   MeSH
• Organelles chemistry   ultrastructure   MeSH
• Computer Simulation MeSH
• Light-Harvesting Protein Complexes chemistry   metabolism   ultrastructure   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Bacteriochlorophylls MeSH
• Carotenoids MeSH
• Light-Harvesting Protein Complexes MeSH