Unsymmetric Chiral Ligands for Large Metallo-Macrocycles: Selectivity of Orientational Self-Sorting.

Nature uses various chiral and unsymmetric building blocks to form substantial and complex supramolecular assemblies. In contrary, majority of organic ligands used in metallosupramolecular chemistry are symmetric and achiral. Here we extend on the group of unsymmetric chiral bile acids used as a scaffold for organic bispyridyl ligands employing the chenodeoxycholic acid (CDCA), epimer of previously used ursodeoxycholic acid (UDCA). Ligands' epimerism, flexibility, and bulkiness leads to large structural differences of coordination products upon reaction with Pd(NO3)2. The UDCA-bispyridyl ligand self-assembles quantitatively into a single crown-like Pd3L6 complex, whereas the CDCA-ligand provides a mixture of coordination complexes of general formula PdnL2n, i.e., Pd2L4, Pd3L6, Pd4L8, Pd5L10, and even Pd6L12 containing impressive 120 chiral centers. The coordination products were studied by a combination of analytical methods, where the ion mobility-mass spectrometry (IM-MS) provided valuable details on their structure and allowed an effective separation of m/z 1461 to individual signals according to arrival time distribution, revealing four different ions of [Pd3L6(NO3)3]3+, [Pd4L8(NO3)4]4+, [Pd5L10(NO3)5]5+, and [Pd6L12(NO3)6]6+. The structures of all complexes were modelled using DFT calculations. Finally, challenges and conclusions in determination of specific structural identity of these unsymmetric species are discussed.

In situ high-resolution structure of the baseplate antenna complex in Chlorobaculum tepidum.

Photosynthetic antenna systems enable organisms harvesting light and transfer the energy to the photosynthetic reaction centre, where the conversion to chemical energy takes place. One of the most complex antenna systems, the chlorosome, found in the photosynthetic green sulfur bacterium Chlorobaculum (Cba.) tepidum contains a baseplate, which is a scaffolding super-structure, formed by the protein CsmA and bacteriochlorophyll a. Here we present the first high-resolution structure of the CsmA baseplate using intact fully functional, light-harvesting organelles from Cba. tepidum, following a hybrid approach combining five complementary methods: solid-state NMR spectroscopy, cryo-electron microscopy, isotropic and anisotropic circular dichroism and linear dichroism. The structure calculation was facilitated through development of new software, GASyCS for efficient geometry optimization of highly symmetric oligomeric structures. We show that the baseplate is composed of rods of repeated dimers of the strongly amphipathic CsmA with pigments sandwiched within the dimer at the hydrophobic side of the helix.

Exciton description of chlorosome to baseplate excitation energy transfer in filamentous anoxygenic phototrophs and green sulfur bacteria.

A description of intra-chlorosome and from chlorosome to baseplate excitation energy transfer in green sulfur bacteria and in filamentous anoxygenic phototrophs is presented. Various shapes and sizes, single and multiwalled tubes, cylindrical spirals and lamellae of the antenna elements mimicking pigment organization in chlorosomes were generated by using molecular mechanics calculations, and the absorption, LD, and CD spectra of these were predicted by using exciton theory. Calculated absorption and LD spectra were similar for all modeled antenna structures; on the contrary, CD spectra turned out to be sensitive to the size and pigment orientations in the antenna. It was observed that, bringing two tubular antennae at close enough interaction distance, the exciton density of the lowest energy state became localized on pigments facing each other in the antenna dimer. Calculations predicted for stacked tubular antenna elements extremely fast, faster than 500 fs, intra-chlorosome energy transfer toward the baseplates in the direction perpendicular to the chlorosome long axis. Downhill excitation energy transfer according to our model is driven by interactions of the antennae with their immediate surroundings. Energy transfer from the chlorosome to the baseplate, consisting of 2D lattices of monomeric and dimeric bacteriochlorophyll a molecules, was predicted to occur in 5-15 ps, in agreement with experimental findings. Advancement of excitation through a double tube antenna stack, a model for antenna element organization in chlorosomes of green sulfur bacteria, to a monomeric baseplate was visualized in space and in time.

Investigation on chlorosomal antenna geometries: tube, lamella and spiral-type self-aggregates.

Molecular mechanics calculations and exciton theory have been used to study pigment organization in chlorosomes of green bacteria. Single and double rod, multiple concentric rod, lamella, and Archimedean spiral macrostructures of bacteriochlorophyll c molecules were created and their spectral properties evaluated. The effects of length, width, diameter, and curvature of the macrostructures as well as orientations of monomeric transition dipole moment vectors on the spectral properties of the aggregates were studied. Calculated absorption, linear dichroism, and polarization dependent fluorescence-excitation spectra of the studied long macrostructures were practically identical, but circular dichroism spectra turned out to be very sensitive to geometry and monomeric transition dipole moment orientations of the aggregates. The simulations for long multiple rod and spiral-type macrostructures, observed in recent high-resolution electron microscopy images (Oostergetel et al., FEBS Lett 581:5435-5439, 2007) gave shapes of circular dichroism spectra observed experimentally for chlorosomes. It was shown that the ratio of total circular dichroism intensity to integrated absorption of the Q(y) transition is a good measure of degree of tubular structures in the chlorosomes. Calculations suggest that the broad Q(y) line width of chlorosomes of sulfur bacteria could be due to (1) different orientations of the transition moment vectors in multi-walled rod structures or (2) a variety of Bchl-aggregate structures in the chlorosomes.