Effect of cationic substitution on the double-well hydrogen-bond potential in [K1-x(NH4)x]3H(SO4)2 proton conductors: a single-crystal neutron diffraction study.

The structure of the mixed crystal [K1-x(NH4)x]3H(SO4)2 as obtained from single-crystal neutron diffraction is compared with the previously reported room-temperature neutron structure of crystalline K3H(SO4)2. The two structures are very similar, as indicated by the high value of their isostructurality index (94.8%). It was found that the replacement of even a small amount (3%) of K+ with NH4+ has a significant influence on the short strong hydrogen bond connecting the two SO42- ions. Earlier optical measurements had revealed that the kinetics of the superionic transition in the solid solution [K1-x(NH4)x]3H(SO4)2 are much faster than in K3H(SO4)2; this reported difference in the kinetics of the superionic phase transition in this class of crystal is explained on the basis of the difference in strength of the hydrogen-bond interactions in the two structures.

Ferroelectric glycine silver nitrate: a single-crystal neutron diffraction study.

Protonated crystals of glycine silver nitrate (C4H10Ag2N4O10) undergo a displacive kind of structural phase transition to a ferroelectric phase at 218 K. Glycine silver nitrate (GSN) is a light-sensitive crystal. Single-crystal X-ray diffraction investigations are difficult to perform on these crystals due to the problem of crystal deterioration on prolonged exposure to X-rays. To circumvent this problem, single-crystal neutron diffraction investigations were performed. We report here the crystal structure of GSN in a ferroelectric phase. The final R value for the refined structure at 150 K is 0.059. A comparison of the low-temperature structure with the room-temperature structure throws some light on the mechanism of the structural phase change in this crystal. We have attempted to explain the structural transition in GSN within the framework of the vibronic theory of ferroelectricity, suggesting that the second-order Jahn-Teller (pseudo-Jahn-Teller) behavior of the Ag(+) ion in GSN leads to structural distortion at low temperature (218 K).

Single-crystal neutron diffraction investigation on crystals belonging to the langasite family: a comparative study.

Crystals of the langasite family are of interest as they are piezoelectric in different devices. The properties of these classes of crystals can be modified within certain limits by isomorphous substitution. Single-crystal neutron diffraction studies were carried out for LGT (La(3)Ga(5.5)Ta(0.5)O(14)), LGST (La(3)Ga(5.25)Ta(0.25)Si(0.5)O(14)) and LGZrT (La(3)Ga(5.25)Ta(0.25)Zr(0.5)O(14)) as the neutron study gives a better average picture of the crystal properties over a macroscopic region of the grown crystal. The effect of small substitutions at various sites on the piezoelectric properties of the crystal was studied.

Investigation of hydrogen-bond network in bis(glycinium) oxalate using single-crystal neutron diffraction and spectroscopic studies.

Single-crystal neutron diffraction investigation of bis(glycinium) oxalate was undertaken in order to study its hydrogen-bonding network, particularly the very short hydrogen bond between the glycinum and oxalate ions, indicated by the X-ray diffraction study. The non-existence of any phase transition in these crystals was attributed to the fact that the short hydrogen bond in bis(glycinium) oxalate is asymmetric in nature, with no hydrogen disorder. The potential energy landscape for the above-mentioned H atom was found to have a single minimum closer to the glycinium ion. IR and Raman investigations of the title complex supported the above result.

Conformation and structure of bis(glycyl-L-aspartic acid) oxalate 0.4-hydrate.

The title bis(glycyl-L-aspartic acid) oxalate complex {systematic name: bis[2-(2-ammonioacetamido)butanedioic acid] oxalate 0.4-hydrate}, 2C6H11N2O5+.C2O4(2-).4H2O, crystallizes in a triclinic space group with the planar peptide unit in a trans conformation. The asymmetric unit consists of two glycyl-L-aspartic acid molecules with positively charged amino groups and neutral carboxyl groups, and an oxalate dianion. The twist around the C-Calpha bond indicates that both the peptide molecules adopt extended conformations, while the twist around the N-Calpha bond shows that one has a folded and the other a semi-extended state. The present complex can be described as an inclusion compound with the dipeptide molecule as the host and the oxalate anion as the guest. The usual head-to-tail sequence of aggregation is not observed in this complex, as is also the case with the glycyl-L-aspartic acid dihydrate molecule. The study of aggregation and interaction patterns in binary systems is the first step towards understanding more complex phenomena. This further leads to results that are of general interest in bimolecular aggregation.

Host-guest interaction in a thiourea-dimethyl oxalate (2/1) complex at 300 and 100 K.

The title complex, 2CH4N2S.C4H6O4, is a host-guest system. The asymmetric unit consists of one complete thiourea molecule and one-half of a dimethyl oxalate molecule lying on an inversion centre. The host thiourea molecules are connected to form zigzag chains by N-H...S hydrogen bonds. The guest dimethyl oxalate molecules provide O-atom acceptors for N-H...O hydrogen bonds, thus interconnecting the chains of thiourea molecules to form completely connected sheets. The reduction in temperature from 300 to 100 K leaves the structure unchanged and still isostructural with that previously determined for the analogous thiourea-diethyl oxalate (2/1) complex. It does, however, induce closer packing of the molecules, general shrinkage of the unit cell and shortening of the hydrogen bonds, these last two to the extent of 1-2%.

Bis(glycinium) oxalate: evidence of strong hydrogen bonding.

In the title 2:1 salt, 2C2H6NO2+.C2O4(2-), the glycine molecule is in the cationic form with a positively charged amino group and an uncharged carboxylic acid group. The doubly charged oxalate anion lies across a crystallographic inversion centre. One of the reasons why the 1:1 glycinium oxalate salt has a higher melting point than the title compound may be the difference in their hydrogen-bonding patterns. A database search for salts formed between amino acids or substituted amino acids and oxalic acid revealed that, in most of the structures, the conformation about the O=C-OH bond is synplanar. D-Tryptophan oxalate is the only example where the OH group of a semi-oxalate adopts an antiplanar conformation. The 2:1 stoichiometry seen in the present salt is observed only in the salts of DL-serine, DL-aspartic acid and betaine with oxalic acid.

Bilateral patellar tendon rupture secondary to repeated local steroid injections.

A case is reported of bilateral patellar tendon rupture in a fit man after a fall. He had a history of repeated local steroid injections into both tendons and histology confirmed steroid-induced changes. The history of repeated local steroid administration has to be implicated as the cause of this extremely rare injury in this patient, which can also be associated with hyperparathyroidism, systemic lupus erythematosus, diabetes and rheumatoid arthritis. All doctors performing repeated local steroid injections into the patellar tendon should be aware of the possible dangers of inducing tendon rupture and should ensure that the steroids are not delivered into its substance.

Enzyme elements involved in the interconversion of L-carbamylaspartate and L-dihydroorotate by dihydroorotase from Clostridium oroticum.

Enzyme elements that are involved in the reversible cyclization of L-carbamylaspartate to L-dihdroorotate catalyzed by dihydroorotase (EC 3.5.2.3) from Clostridium oroticum (ATCC 25750) have been studied. Removal of Zn(II) from the enzyme by chelators followed by incubation of apoenzyme with Co(II) results in replacement of two to three of the four Zn(II) ions per molecule by Co(II). The catalytic properties of the Zn(II)Co(II) dihydroorotase are different from those of native enzyme. The Vmax is increased for both the synthesis and hydrolysis of L-dihydroorotate. The Km for L-dihydroorotate is unchanged, while the Km for L-carbamylaspartate is increased more than twofold. On the other hand, the kinetic properties of Zn(II)-reconstituted dihydroorotase are indistinguishable from those of native enzyme. The pH dependence of Vmax is also altered by the Co(II) substitution. For both Zn(II)- and Zn(II)Co(II)-dihydroorotase, this pH dependence is well described by a single ionization and the pK's for L-dihydroorotate synthesis and hydrolysis are different. Substitution with Co(II) increases the pK for both reaction directions to different extents. These results strongly support a role for the tightly bound metals in the catalytic mechanism. In addition, diethylpyrocarbonate rapidly inactivates the enzyme. The inactivation is prevented by L-dihydroorotate. This result is consistent with a role for at least one histidine in catalysis. The possibility that C. oroticum dihydroorotase may be useful model for the more complex mammalian enzyme is considered.