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Nina Lah

Publications and source records attributed to Nina Lah.

5 recordsLinked to original sources

A dimeric cobalt(II)-suberate complex with 3-aminopyridine.

The title complex, mu-octane-1,8-dioato-bis[bis(3-aminopyridine)chloro(methanol)cobalt(II)], [Co2(C8H12O4)Cl2(C5H6N2)4(CH4O)2], is located on a crystallographic centre of inversion. The coordination around each of the Co centres is distorted octahedral, involving two N, three O and one Cl atom. Discrete dimers are connected in a three-dimensional arrangement through N-H...O, N-H...Cl and O-H...O hydrogen-bond interactions.

Journal Article↗

The solution structures and dynamics and the solid-state structures of substituted cyclopentadienyltitanium(IV) trifluorides.

Organotitanium fluorides (C5Me4R)TiF3 (R = H, Me, Et) sublimate with formation of crystalline dimers. From solution, we obtained crystals of dimers and tetramers. The tetramer [{(C5Me5)TiF3}4] irreversibly dissociates in the solid state to dimers (DeltaH = 8.33 kcal mol(-1)). The variable-temperature (1)H and (19)F NMR spectroscopy measurements of the toluene-d(8) solution of [{(C5Me5)TiF3}2] revealed at 202 K one monomeric, two dimeric (with C2h and Cs symmetry), two tetrameric (with D2 and C2v symmetry), and two trimeric (both C2 symmetry) molecules. With the increase in temperature and dilution of the solution, the composition of the solution shifts to the smaller molecules. The thermodynamic and activation parameters for the reversible dissociation of dimers to monomers in the solution are DeltaH = 9.2 kcal mol(-1), DeltaS = 24.2 cal mol(-1) K(-1), DeltaH(double dagger) = 12.2 kcal mol(-1), DeltaS(double dagger) = 9.7 cal mol(-1) K(-1). The dissociation path with a weakly double-bridged transition-state dimer was proposed. The thermodynamic parameters for the reversible dissociation of the C2v tetramer to the dimers in solution are DeltaH = 7.9 kcal mol(-1) and DeltaS = 26.8 cal mol(-1) K(-1). From both tetramers, the D2 molecule is 0.34(5) kcal mol(-1) lower in enthalpy and 6.5(5) cal mol(-1) K(-1) lower in entropy than the C2v molecule. The structures of both trimers were proposed. The low-temperature 19F NMR spectra of the CDCl3 solution of [{(C5Me5)TiF3}2] are consistent with equilibria of a monomer, two dimers (with C2h and Cs symmetry), and a trimer. The vapor pressure osmometric molecular mass determination of CDCl3 solution of [{(C5Me5)TiF3}2] at 302 K is consistent with the equilibrium of the dimer and the monomer.

Journal Article↗

4-aminopyridinium hydrogen maleate.

The title compound, C(5)H(7)N(2)(+)...C(4)H(3)O(4)(-), crystallizes in space group P2(1) with one ion pair in the asymmetric unit. The hydrogen maleate anion possesses nearly planar geometry and displays an extremely short intramolecular O--H...O hydrogen bond, with an O...O distance of 2.4198 (19) A. Classical N-H...O hydrogen bonds, together with short C--H...O contacts, generate an extensive hydrogen-bonding network.

Journal Article↗

2-aminothiazole and 2-aminothiazolinone derivatives.

The reaction of different substituted alpha-cyanooxiranes with thiourea resulted in the formation of the 2-aminothiazolinone derivative 2-amino-5-(2,5-dimethoxyphenyl)-1,3-thiazol-4(5H)-one, C(11)H(12)N(2)O(3)S, (I), and the 2-aminothiazole derivative ethyl 2-amino-5-(2,5-dimethoxyphenyl)-1,3-thiazole-4-carboxylate, C(14)H(16)N(2)O(4)S, (II). The geometries of the two crystallographically independent molecules in (II) are nearly identical but mirror related. The crystal structures of both compounds contain two types of intermolecular hydrogen bonds.

Crystallography, X-Ray↗

Specific potassium binding stabilizes pI258 arsenate reductase from Staphylococcus aureus.

Arsenate reductase (ArsC) from Staphylococcus aureus plasmid pI258 catalyzes the reduction of arsenate to arsenite and plays a role in bacterial heavy metal resistance. The high resolution x-ray structure of ArsC reveals the atomic details of the K+ binding site situated next to the catalytic P-loop structural motif of this redox enzyme. A full thermodynamic study of the binding characteristics of a series of monovalent cations (Li+, Na+, K+, Rb+, and Cs+) and their influence on the thermal stability of ArsC was performed with isothermal titration calorimetry, circular dichroism spectroscopy, and differential scanning calorimetry. Potassium has the largest affinity with a Ka of 3.8 x 10(3) m(-1), and the effectiveness of stabilization of ArsC by monovalent cations follows the binding affinity order: K+ > Rb+ > Cs+ > Na+ > Li+. A mutagenesis study on the K+ binding side chains showed that Asn-13 and Asp-65 are essential for potassium binding, but the impact on the stability of ArsC was the most extreme when mutating Ser-36. Additionally, the thermal stabilization by K+ is significantly reduced in the case of the ArsC E21A mutant, showing the importance of a Glu-21-coordinated water molecule in its contact with K+. Although potassium is not essential for catalysis, in its presence the kcat/KM increases with a factor of 5. Altogether, the interaction of K+ with specific residues in ArsC is an enthalpydriven process that stabilizes ArsC and increases the specific activity of this redox enzyme.

Arsenite Transporting ATPases↗