Unexpected Participation of the Carbonate Anion in the Assembly of Hexanuclear Cadmium(II) Trimethylacetate Complex

2020 ◽  
Vol 46 (8) ◽  
pp. 553-556
Author(s):  
G. N. Kuznetsova ◽  
D. S. Yambulatov ◽  
M. A. Kiskin ◽  
N. V. Gogoleva ◽  
M. A. Shmelev ◽  
...  
Keyword(s):  
2016 ◽  
Vol 52 (62) ◽  
pp. 9628-9631 ◽  
Author(s):  
Xuezhao Li ◽  
Jinguo Wu ◽  
Liyong Chen ◽  
Xiaoming Zhong ◽  
Cheng He ◽  
...  

Quantitative dynamic capsule–capsule conversion by cooperative binding one carbonate anion and switchable dual catalysis was achieved within an Ir2Co3-type capsule.


2006 ◽  
Vol 101 (4) ◽  
pp. 2371-2376 ◽  
Author(s):  
Zhaoqiang Wu ◽  
Lingzhi Meng ◽  
Cheng Li ◽  
Xiaoju Lu ◽  
Lifen Zhang ◽  
...  

1986 ◽  
Vol 32 (11) ◽  
pp. 847-854 ◽  
Author(s):  
G. Dennis Sprott ◽  
Terry J. Beveridge ◽  
Girishchandra B. Patel ◽  
Giulio Ferrante

Sheaths of Methanospirillum hungatei are very resilient structures and consist of circumferential rings, which have been likened to the hoops of a barrel. The isolated sheaths are dramatically disassembled to the individual hoops upon treatment with β-mercaptoethanol at 90 °C. Sheath disassembly resulted in a large decrease in suspension turbidity and a release of approximately 10% of sheath protein in the form of 4.6 to 7.0 kiloDalton (kDa) peptides. These are referred to as "glue peptides" to suggest a function in linking the hoops together to form the intact sheath. The liberated hoops consisted of a protein surface array crystallized on a matrix material. Intact sheaths, or hoops largely freed of the glue peptides, could be solubilized at 90 °C by (i) a combination of β-mercaptoethanol and sodium dodecyl sulfate, (ii) by alkaline conditions of pH 12 or more, or partially (iii) by carbonate anion at pH 11. Fractionation by liquid chromatography of hoops solubilized by alkaline conditions of pH 12.6 revealed major polypeptides of about 24 and 45 kDa; a smaller peak occurred at 12 kDa. Based on the dimensions of the unit cell of the crystalline array, we suggest that two copies of the 24-kDa polypeptide form the 5.6 × 2.8 nm unit cell as a dimer, which then tends to form larger aggregates. The 2.8-nm subunit may be a dimer of the 12-kDa species. Sheaths of M. hungatei strain JF1 exhibited a similar polypeptide profile, but in this case, the 45-kDa species predominated.


2013 ◽  
Vol 101 ◽  
pp. 18-26 ◽  
Author(s):  
Gangulibabu ◽  
Kalaiselvi Nallathamby ◽  
Danielle Meyrick ◽  
Manickam Minakshi

2014 ◽  
Vol 70 (5) ◽  
pp. m160-m161 ◽  
Author(s):  
Niels-Patrick Pook ◽  
Mimoza Gjikaj ◽  
Arnold Adam

The complex cation of the title compound, [Co(CO3)(C10H8N2)2]2(C12H10N2O6)·6H2O, contains a CoIIIatom with a distorted octahedral coordination environment formed by four N atoms from two bidentate 2,2′-bipyridine ligands and one bidentate carbonate anion. The asymmetric unit is completed by one-half of the 2-({4-[(carboxylatomethyl)carbamoyl]phenyl}formamido)acetate dianion, which is located on a centre of inversion, and by three water molecules. Two [Co(CO3)(C10H8N2)2]+cations are connected through C—H...O contacts by the uncoordinating anions. The aromatic rings of the 2,2′-bipyridine ligands and diacetate anions are involved in π–π stacking and C—H...π interactions. The centroid–centroid distances are in the range 3.4898 (4)–3.6384 (5) Å. The crystal structure is stabilized by further O—H...O and N—H...O hydrogen bonds, which give rise to a three-dimensional supramolecular network.


2019 ◽  
Vol 75 (8) ◽  
pp. 1182-1187 ◽  
Author(s):  
Akiko Asano ◽  
Mitsinobu Doi

The four azole rings place structural restrictions on ascidiacyclamide (ASC). As a result, the structure of ASC exists in an equilibrium between two major forms (i.e. folded and square). [D-βVal3,7]Ascidiacyclamide (βASC) was synthesized by replacing two D-Val-Thz (Val is valine and Thz is thiazole) blocks with D-β-Valine (D-βVal-Thz). This modification expands the peptide ring; the original 24-membered macrocycle of ASC becomes a 26-membered ring. Circular dichroism (CD) spectra showed that, in solution, the structural equilibrium is maintained with βASC, but the folded form is dominant. A copper complex was prepared, namely [[D-βVal3,7]ascidiacyclamide(2−)]aqua-μ-carbonato-dicopper(II) monohydrate, [Cu2(C38H54N8O6S2)(CO3)(H2O)]·H2O, to determine the effect of the change in ring size on the coordinated structure. The obtained bis-CuII–βASC complex contains two water molecules and a carbonate anion. Two CuII ions are chelated by three N-donor atoms of two Thz–Ile–Oxz (Ile is isoleucine and Oxz is oxazoline) units. An O atom of the carbonate anion bridges two CuII ions, forming two square pyramids. These features are similar to the previously reported structure of the CuII–ASC complex, but the two pyramids are enveloped inside the peptide and share one apex. In the CuII–ASC complex, the apex of each square pyramid is an O atom of a water molecule, and the two pyramids are oriented toward the outside of the peptide. The incorporated β-amino acids of βASC make the space inside the peptide large enough to envelop the two square pyramids. The observed structural changes in the bis-CuII–βASC complex arising from ring expansion are particularly interesting in the context of the previously reported structure of the CuII–ASC complex.


1994 ◽  
Vol 49 (10) ◽  
pp. 1368-1372 ◽  
Author(s):  
Yue Qing Zheng ◽  
Arnold Adam

Abstract The new complex carbonate Rb2[Mg(CO3)2(H2O))4] crystallizes in the Baylissite-type structure with a = 1130,4(3), b = 641,9(1), c = 703,3(2) pm, β = 99,62(1)°, VEZ = 503,2(2), space group P21/n (No. 14) and Z = 2. In comparison with the isostructural potassium compound the cell dimensions increase in b- and c- and decrease in a-direction. This effect depends on the greater coordination number of Rb+ and the rigidity of strong hydrogen bonds. The carbonate anion exhibits significant deviations from D3h-symmetry (C -O: 127,1(5)-130,2(5) pm, ∠ O - C - O: 117,9(4)-121,1(3)°).


2003 ◽  
Vol 417 (2) ◽  
pp. 165-175 ◽  
Author(s):  
J.Matthew Hutzler ◽  
Frank J Powers ◽  
Michael A Wynalda ◽  
Larry C Wienkers

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