Assembly Of Chlorophyll Research Articles

Dendron-mediated control over self-assembly of chlorophyll rosettes into columnar vs. discrete aggregates

By controlling the π-π stacking of chlorophyll supramolecular rosettes through steric hindrance of alkyl dendrons, it become possible to create chlorophyll tubes and discrete rings that resemble to natural chlorophyll assemblies.

A Light-Harvesting/Charge-Separation Model with Energy Gradient Made of Assemblies of meta-Pyridyl Zinc Porphyrins.

Self-assembly of porphyrins is a fascinating topic, not only for mimicking chlorophyll assemblies in photosynthetic organisms, but also for the potential of creating molecular-level devices. Herein, zinc porphyrin derivatives bearing a meta-pyridyl group at the meso position were prepared and their assemblies studied in chloroform. Among the porphyrins studied, one with a carbamoylpyridyl moiety gave a distinct 1 H NMR spectrum in CDCl3 , which allowed the supramolecular structure in solution to be probed in detail. Ring-current-induced chemical-shift changes in the 1 H NMR spectrum, together with vapor-pressure osmometry and diffusion-ordered NMR spectroscopy, among other evidence, suggested that the porphyrin molecules form a trimer with a triangular cone structure. Incorporation of a directly linked porphyrin-ferrocene dyad with the same assembling properties in the assemblies led to a rare example of a light-harvesting/charge-separation system in which an energy gradient is incorporated and reductive quenching occurs.

Light polarization dependency existing in the biological photosystem and possible implications for artificial antenna systems.

The processes of biological photosynthesis provide inspiration and valuable lessons for artificial energy collection, transfer, and conversion systems. The extraordinary efficiency of each sequential process of light to biomass conversion originates from the unique architecture and mechanism of photosynthetic proteins. Near 100% quantum efficiency of energy transfer in biological photosystems is achieved by the chlorophyll assemblies in antenna complexes, which also exhibit a significant degree of light polarization. The three-dimensional chiral assembly of chlorophylls is an optimized biological architecture that enables maximum energy transfer efficiency with precisely designed coupling between chlorophylls. In this review, we summarize the key lessons from the photosynthetic processes in biological photosystems, and move our focus to energy transfer mechanisms and the chiral structure of the chlorophyll assembly. Then, we introduce recent approaches and possible implications to realize the biological energy transfer processes on bioinspired scaffold-based artificial antenna systems.

Photoactive nanocomplex formed from chlorophyll assembly on TMA-coated iron oxide nanoparticles

In this study, hierarchical self-assembly of photocatalytic nanodisks through non-covalent interactions between spinach-extracted chlorophyll molecules and trimethylammonium hydroxide-coated magnetic iron oxide nanoparticles was discussed. Combination of chlorophyll molecules with iron oxide nanoparticles generated an alteration in light absorption at both visible and near-IR region with accompanying enhancement in fluorescence emission. Further, photocatalytic role of resulting molecular assembly was studied by means of the photoinduced degradation of methylene blue dye under UV light and direct sun irradiation at neutral pH. In order to enhance the long-term stability of the hybrid nanocatalyst, commercially available cellulose membrane was used as a support and magnetic recovery and reusability was achieved where the nanocatalyst retained more than 90 % of its efficiency even after four cycles. This simple strategy could initiate the development of new materials for wastewater treatment including membrane-based technologies. On the other hand, their sunlight-induced photocatalytic activity could easily be conducted to dye-synthesized solar cells or their enhanced photoluminescence can provide a strong basis for future bioimaging tools.

Assemblies of ionic zinc chlorins assisted by water-soluble polypeptides

Artificial chlorophyll–peptide complexes were prepared by mixing ionic chlorophyll derivatives and oligopeptides in aqueous media containing a small amount of organic solvent. The pigment–peptide complexes provided chlorophyll assemblies showing a sharp red-shifted Qy absorption band concomitant with giant circular dichroism signals. The polypeptide-assisted assemblies of chlorophyllous pigments would afford a good model for photosynthetic apparatuses such as pigment–protein complexes of light-harvesting antennas.

Construction of dendrimers with a square-shaped core consisting of zinc chlorophyll assembly via intermolecular nitrogen–zinc coordination

The first dendrimers consisting of self-assembled zinc chlorophyll derivatives are reported. Coordination-directed self-assembly of pyridine-appended zinc chlorophyll derivatives tethering a dendron moiety results in cyclic tetramers peripherally functionalized by dendrons via intermolecular axial coordination interaction between the nitrogen atom in the pyridine ring and the zinc atom in the chlorin ring. We characterized the formation of the cyclic tetramers by use of 1H NMR measurements including diffusion-ordered spectroscopy (DOSY). Four different types of dendrons were introduced in the zinc chlorophyll component to investigate the tolerance of the self-assembly to the dendron structure. All dendrimers exhibited similar stabilities, which demonstrates that the dendron moiety does not interfere with the self-assembly, such that more than 90% of the molecules are in the assembly at concentrations >0.2mM in benzene.

Assembly of water-soluble chlorophyll-binding proteins with native hydrophobic chlorophylls in water-in-oil emulsions

The challenges involved in studying cofactor binding and assembly, as well as energy- and electron transfer mechanisms in the large and elaborate transmembrane protein complexes of photosynthesis and respiration have prompted considerable interest in constructing simplified model systems based on their water-soluble protein analogs. Such analogs are also promising templates and building blocks for artificial bioinspired energy conversion systems. Yet, development is limited by the challenge of introducing the essential cofactors of natural proteins that are highly water-insoluble into the water-soluble protein analogs. Here we introduce a new efficient method based on water-in-oil emulsions for overcoming this challenge. We demonstrate the effectiveness of the method in the assembly of native chlorophylls with four recombinant variants of the water-soluble chlorophyll-binding protein of Brassicaceae plants. We use the method to gain new insights into the protein–chlorophyll assembly process, and demonstrate its potential as a fast screening system for developing novel chlorophyll–protein complexes.

Construction of chlorophyll assemblies based on zinc complexes of triazole–chlorin conjugates

A series of triazole–chlorin conjugates were prepared by Huisgen reactions of a C3–ethynylated chlorophyll derivative with azido compounds. Dimerization behaviour of their zinc complexes was investigated based on UV–vis, circular dichroism, and 1H NMR spectroscopies as well as molecular modelling calculation.

The Collapse of the Tyrosine Z•−Mn Spin−Spin Interaction above ∼100 K Reveals the Spectrum of Tyrosine Z•. An Application of Rapid-Scan EPR to the Study of Intermediates of the Water Splitting Mechanism of Photosystem II

Tyr Z of photosystem II mediates electron transfer from the water splitting site, a Mn4Ca cluster, to the specialized chlorophyll assembly P680. Due to its proton-limited redox properties and the proximity to the Mn cluster, it is thought to play a critical role in the proton-coupled electron transfer reactions that constitute the four-step oxidation mechanism (so-called S-state transitions) of water to molecular oxygen. Spectroscopic evidence for the Tyr Z radical has been scarce in intact preparations (it is difficult to probe it optically, and too short-lived for EPR characterization) until recently. Advances in recent years have allowed the trapping at liquid helium temperatures and EPR characterization of metalloradical intermediates, attributed to tyrosyl Z* magnetically interacting with the Mn cluster. We have extended these studies and examined the evolution of the spectra of five intermediates: S0YZ*, S0YZ* (with 5% MeOH), S1YZ*, S2YZ*, and S2YZ* (with 5% MeOH) in the temperature range of 11-230 K. A rapid-scan EPR method has been applied at elevated temperatures. The tyrosyl radical decouples progressively from Mn, as the Mn relaxation rate increases with an increase in temperature. Above approximately 100 K, the spectra collapse to the unperturbed spectrum of Tyr Z*, which is found to be somewhat broader than that of the stable Tyr D* radical. This study provides a simple means for recording the spectrum of Tyr Z* and extends earlier observations that link the photochemistry at liquid helium temperatures to the photochemistry at temperatures that support S-state transitions.

Photochemical Competence of Assembled Photosystem II Core Complex in Cyanobacterial Plasma Membrane

Cyanobacterial cells have two autonomous internal membrane systems, plasma membrane and thylakoid membrane. In these oxygenic photosynthetic organisms the assembly of the large membrane protein complex photosystem II (PSII) is an intricate process that requires the recruitment of numerous protein subunits and cofactors involved in excitation and electron transfer processes. Precise control of this assembly process is necessary because electron transfer reactions in partially assembled PSII can lead to oxidative damage and degradation of the protein complex. In this communication we demonstrate that the activation of PSII electron transfer reactions in the cyanobacterium Synechocystis sp. PCC 6803 takes place sequentially. In this organism partially assembled PSII complexes can be detected in the plasma membrane. We have determined that such PSII complexes can undergo light-induced charge separation and contain a functional electron acceptor side but not an assembled donor side. In contrast, PSII complexes in thylakoid membrane are fully assembled and capable of multiple turnovers. We conclude that PSII reaction center cores assembled in the plasma membrane are photochemically competent and can catalyze single turnovers. We propose that upon transfer of such PSII core complexes to the thylakoid membrane, additional proteins are incorporated followed by binding and activation of various donor side cofactors. Such a stepwise process protects cyanobacterial cells from potentially harmful consequences of performing water oxidation in a partially assembled PSII complex before it reaches its final destination in the thylakoid membrane.

Conversion of Chlorophyll b to Chlorophyll a and the Assembly of Chlorophyll with Apoproteins by Isolated Chloroplasts.

The photosynthetic apparatus is reorganized during acclimation to various light environments. During adaptation of plants grown under a low-light to high-light environment, the light-harvesting chlorophyll a/b-protein complexes decompose concomitantly with an increase in the core complex of photosystem II. To study the mechanisms for reorganization of photosystems, the assembly of chlorophyll with apoproteins was investigated using isolated chloroplasts. When [14C]chlorophyllide b was incubated with chloroplasts in the presence of phytyl pyrophosphate, it was esterified and some of the [14C]chlorophyll b was converted to [14C]chlorophyll a via 7-hydroxymethyl chlorophyll. [14C]Chlorophyll a and b were incorporated into chlorophyll-protein complexes. Light-harvesting chlorophyll a/b-protein complexes of PSII had a lower [14C]chlorophyll a to [14C]chlorophyll b ratio than P700-chlorophyll a-protein complexes, indicating the specific binding of chlorophyll to apoproteins in our systems. 7-Hydroxymethyl chlorophyll, an intermediate molecule from chlorophyll b to chlorophyll a, did not become assembled with any apoproteins. These results indicate that chlorophyll b is released from light-harvesting chlorophyll a/b-protein complexes of photosystem II and converted to chlorophyll a via 7-hydroxymethyl chlorophyll in the lipid bilayer and is then used for the formation of core complexes of photosystems. These mechanisms provide the fast, fine regulation of the photosynthetic apparatus during construction of photosystems.

Effect of Supplementary UVB Radiation on Chlorophyll Synthesis and Accumulation of Photosystems during Chloroplast Development in Spirodela oligorrhiza

Abstract— Although the effects of ultraviolet B (UVB, 290–320 nm) radiation have been studied in plants extensively, little is known about the potential impacts on maturation of chloroplasts. To address this problem, the effects of supplementary UVB on chloroplast development were examined in the aquatic higher plant Spirodela oligorrhiza. Dark‐grown Spirodela‐containing proplastids were exposed to photosynthetically active radiation (PAR) and ultraviolet A (UVA, 320–400 nm), plus supplementary UVB equivalent to 1% of PAR on a photon basis. The biosynthesis and assembly of chlorophyll (Chi) into reaction centers was followed for 4 days in situ by low temperature (77 K) Chi fluorescence. Impacts on chloroplast development were detected after only 1 h incubation in light with supplementary UVB. Fluorescence emission signals from Chi associated with the photosystem (PS) II antenna, PSII reaction centers and PSI reaction centers were detected at the same time with or without UVB, but the magnitude of PS fluorescence was diminished up to 60% in plants incubated in UVB. The Chi content was also lower in UVB‐treated plants, but to a lesser degree than anticipated by low temperature fluorescence, suggesting lack of organization and/or association of Chi with PS. Electron transport, measured with room temperature fluorescence induction, was not consistently different in plants exposed to UVB. These results suggest that with UVB, fewer and/or smaller PS form during chloroplast development, but there is not a large inhibition of Chi synthesis or PSII activity.

Localization and Characterization of Photosystem II in Grana and Stroma Lamellae

Attempts have been made to identify intramembranous particles observed in freeze-fracture electron microscopy as specific functional components of the membrane. The intramembranous particles of the exoplasmic fracture (EF) face of freeze-fractured pea (Pisum sativum) chloroplast lamellae are nonuniformly distributed along the membrane. Approximately 20% of the particles are in unpaired membrane regions whereas 80% are localized in regions of stacked lamellae (grana partitions). The EF particles within the grana regions of the chloroplast membrane are of a larger average size than those in stroma lamellae.Photosystem II activity of isolated stroma lamellae is about 20 to 25% of that of grana-enriched membrane fragments when measured at high light intensities. The photosystem II activity of stroma lamellae requires higher light intensities for attainment of maximal rates than does that of grana membranes. Lactoperoxidase-catalyzed iodination of stacked chloroplast lamellae was used to demonstrate that 75 to 80% of all photosystem II centers are localized in grana partition regions.The data presented support the concept that the intramembranous particles of the EF face visualized on freeze-fractured chloroplast lamellae represent a central photosystem II reaction center complex plus associated light-harvesting chlorophyll protein. The fact that the EF particles of stroma lamellae are smaller than those of grana regions can be directly correlated to the presence of photosystem II units with small antennae chlorophyll assemblies in stroma lamellae.