David Keen

Abstract:

Using a combination of single-crystal neutron scattering and reverse Monte Carlo refinements, we study the magnetic structure of paramagnetic MnO at a temperature (160 K) substantially below the Curie-Weiss temperature |θ|∼550 K. The microscopic picture we develop reveals a locally ordered domain structure that persists over distances many times larger than the correlation length implied by direct analysis of the spin-correlation function. Moreover, the directional dependence of paramagnetic spin correlations in paramagnetic MnO differs in some important respects from that of its incipient ordered antiferromagnetic state. Our results demonstrate that atomistic refinement to large three-dimensional neutron-scattering datasets is a practical approach, and have implications for the understanding of paramagnetic states in weakly frustrated systems, including high-temperature superconductors.

Abstract:

Metal-organic frameworks (MOFs) are a family of chemically diverse materials, with applications in a wide range of fields, covering engineering, physics, chemistry, biology and medicine. Until recently, research has focused almost entirely on crystalline structures, yet now a clear trend is emerging, shifting the emphasis onto disordered states, including 'defective by design' crystals, as well as amorphous phases such as glasses and gels. Here we introduce a strongly associated MOF liquid, obtained by melting a zeolitic imidazolate framework. We combine in situ variable temperature X-ray, ex situ neutron pair distribution function experiments, and first-principles molecular dynamics simulations to study the melting phenomenon and the nature of the liquid obtained. We demonstrate from structural, dynamical, and thermodynamical information that the chemical configuration, coordinative bonding, and porosity of the parent crystalline framework survive upon formation of the MOF liquid.

Abstract:

Enzymes dependent on pyridoxal 5'-phosphate (PLP, the active form of vitamin B₆) perform a myriad of diverse chemical transformations. They promote various reactions by modulating the electronic states of PLP through weak interactions in the active site. Neutron crystallography has the unique ability of visualizing the nuclear positions of hydrogen atoms in macromolecules. Here we present a room-temperature neutron structure of a homodimeric PLP-dependent enzyme, aspartate aminotransferase, which was reacted in situ with α-methylaspartate. In one monomer, the PLP remained as an internal aldimine with a deprotonated Schiff base. In the second monomer, the external aldimine formed with the substrate analog. We observe a deuterium equidistant between the Schiff base and the C-terminal carboxylate of the substrate, a position indicative of a low-barrier hydrogen bond. Quantum chemical calculations and a low-pH room-temperature X-ray structure provide insight into the physical phenomena that control the electronic modulation in aspartate aminotransferase.Pyridoxal 5'-phosphate (PLP) is a ubiquitous co factor for diverse enzymes, among them aspartate aminotransferase. Here the authors use neutron crystallography, which allows the visualization of the positions of hydrogen atoms, and computation to characterize the catalytic mechanism of the enzyme.