Ring-shaped Trimer Research Articles

{Ti6}/{Ti10} Wheel Cluster Substituted Silicotungstate Aggregates.

Two novel Ti-oxo wheel cluster substituted silicotungstates (STs) [H2N(CH3)2]9H9[Ti6O6(SiW10O37)3]·11H2O (1) and [H2N(CH3)2]16H10[Ti10O11(SiW10O37)2(SiW9O35)2]·14H2O (2) have been made by hydrothermal reactions. The polyoxoanion of 1 is a ring-shaped trimer where a Ti6O6 ({Ti6}) wheel cluster is encapsulated by three divacant [SiW10O37]10- (SiW10O37) fragments. However, 2 is built by two divacant SiW10O37 units and two rare trivacant [SiW9O35]12- (SiW9O35) fragments and further installs an unprecedented Ti10O11 ({Ti10}) double-wheel cluster. To the best of our knowledge, 2 is rare in POM chemistry. Studies on the catalytic oxidation properties reveal that 1 exhibits high catalytic activity toward the oxidation of various sulfides using H2O2 as an oxidant. Furthermore, 1 can be facilely recycled and reused for at least five cycles without obvious loss of catalytic activity.

Functional roles of the hexamer structure of C-phycocyanin revealed by calculation of absorption wavelength.

Cyanophyta-phycocyanin (C-PC) is the main constituent of the rod of phycobilisome (PBS), which is a highly ordered and large peripheral light-harvesting protein complex present on the cytoplasmic side of the thylakoid membrane in cyanobacteria and red algae. The C-PC monomer comprises two chains, α- and β-subunits, and aggregates to form ring-shaped trimers (αβ)3 with rotational symmetry. The ring-shaped trimer (αβ)3 is a structural block unit (SBU) that forms the rod of PBS. Two (αβ)3 SBUs are arranged in a face-to-face manner to form an (αβ)6 -hexamer. In this study, the electronic states of three phycocyanobilins, α84, β84, and β155 in C-phycocyanin, constituting the rod of the PBS, were calculated for both the trimer and hexamer models by considering the effect of the electrostatic field of protein moieties and water molecules. For the hexamer, the absorption wavelengths of α84, β84, and β155 were similar to those obtained experimentally; however, for the trimer, only the absorption wavelength of β155 shifted toward a shorter-wavelength. The nature of the hexamer structure as a hierarchical structure is revealed by considering the calculated absorption wavelength and energy transfer.

Quantum master equation approach to singlet fission dynamics in pentacene ring-shaped aggregate models.

The quantum master equation approach is applied to the singlet fission (SF) dynamics of pentacene ring-shaped aggregate models to clarify the Frenkel excitonic (FE) coupling effects on the SF rate and correlated-triplet pair (TT) yield as well as their dependences on the aggregate structure and size. Interestingly, the smallest ring model, a ring-shaped trimer, is found to exhibit a significantly smaller SF rate and a slightly smaller TT yield than those of the dimer model with the same intermonomer interaction and to show remarkable variations in the SF dynamics with increasing the FE coupling. With increasing the size of the aggregates with FE coupling, it is found that the SF rate rapidly increases, attains the maximum at 17-mer (∼3 times enhancement compared to the non-FE-coupling case), and then decreases, approaching a stationary value around 25-mer, while the almost stationary TT yield at 25-mer remains 16% smaller than that in the non-FE-coupling case. These features are found to be in qualitative agreement with those in the corresponding linear aggregates, although the aggregate size gives a maximum SF rate, and the values of the maximum SF rate as well as of the converged TT yield are different between the ring-shaped and linear aggregates. These results are interpreted based on the relative relaxation factors between the adiabatic exciton states as well as on the vibronic coupling effects. The present results contribute to a deeper understanding of the aggregate structure and size dependences of SF dynamics and to constructing the design guidelines for highly efficient SF aggregates.

A ring-shaped hemoprotein trimer thermodynamically controlled by the supramolecular heme-heme pocket interaction.

Engineered cytochrome b562, a small hemoprotein, with an externally-attached heme moiety via a moderately long linker at a suitable position predominantly forms a thermodynamically stable ring-shaped trimer in dilute solution. In an equilibrium between supramolecular polymerization and depolymerization, the ring-shaped trimer is kinetically trapped even in a concentrated solution.

Simultaneous interactions of amphoteric halogen in XY (X = Cl, Br and Y = F, Cl, Br) with C and O atoms of CO2 in ring-shaped CO2·X(Y)·CO2 complexes

Dihalogen molecule XY (X=Cl and Br and Y=F, Cl and Br) can interact with two CO2 and form ring-shaped CO2·X(Y)·CO2 trimers, in which the X atom simultaneously interacts with C atom of one CO2 and O atom of the other CO2. Theoretical calculations show that their optimized geometries and stretching vibrational frequencies are different from the individual (CO2)2, CO2⋯XY and YX⋯CO2 dimers. Their interaction energies are stronger than the sum of the interaction energies of the individual dimers, revealing the cooperativity between the dimers. Their binding distances and interaction strengths are closely associated with the electronegativity of X and Y atoms. Energy decomposition analysis suggests that electrostatic force is the main net contribution to total interaction energy. Quantum theory of atoms in molecules analysis confirms the formation of ring-shaped structures and the cooperativity between the dimers. Molecular electrostatic potential was employed to elucidate the formation mechanisms of ring-shaped trimers.

A charged residue at the subunit interface of PCNA promotes trimer formation by destabilizing alternate subunit interactions.

Eukaryotic proliferating cell nuclear antigen (PCNA) is an essential replication accessory factor that interacts with a variety of proteins involved in DNA replication and repair. Each monomer of PCNA has an N-terminal domain A and a C-terminal domain B. In the structure of the wild-type PCNA protein, domain A of one monomer interacts with domain B of a neighboring monomer to form a ring-shaped trimer. Glu113 is a conserved residue at the subunit interface in domain A. Two distinct X-ray crystal structures have been determined of a mutant form of PCNA with a substitution at this position (E113G) that has previously been studied because of its effect on translesion synthesis. The first structure was the expected ring-shaped trimer. The second structure was an unanticipated nontrimeric form of the protein. In this nontrimeric form, domain A of one PCNA monomer interacts with domain A of a neighboring monomer, while domain B of this monomer interacts with domain B of a different neighboring monomer. The B-B interface is stabilized by an antiparallel beta-sheet and appears to be structurally similar to the A-B interface observed in the trimeric form of PCNA. The A-A interface, in contrast, is primarily stabilized by hydrophobic interactions. Because the E113G substitution is located on this hydrophobic surface, the A-A interface should be less favorable in the case of the wild-type protein. This suggests that the side chain of Glu113 promotes trimer formation by destabilizing these possible alternate subunit interactions.

Crystallization and preliminary X-ray diffraction analysis of the light-harvesting protein phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus.

The crystallization and preliminary crystallographic study of phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus is reported. Phycocyanin is composed of alpha- and beta-subunits consisting of 162 and 172 amino-acid residues, respectively. These associate to form an alphabeta heterodimer, which further associates to give a ring-shaped trimer (alphabeta)(3). Two trimers bind head-to-head to form a hexamer (alphabeta)(6). Phycocyanin crystals have been obtained by the sitting-drop vapour-diffusion method with a precipitant solution containing 30%(w/v) PEG 4000 and 100 mM MES pH 7.5-8.0. Using synchrotron radiation, the crystals diffract to 2.0 A resolution. They belong to the trigonal space group R32, with unit-cell parameters a = b = 186.75 (3), c = 59.75 (4) A, alpha = beta = 90, gamma = 120 degrees. Assuming that the crystallographic triad is identical to the threefold axis of the hexamer and with three (alphabeta)(6) molecules in a unit cell, the calculated molar volume (V(M)) is 2.64 A(3) Da(-1). This value corresponds to a solvent content of approximately 53%, with one alphabeta heterodimer occupying the asymmetric unit.