X-ray and neutron scattering

Abstract:

Conversion of aldo to keto sugars by the metalloenzyme D-xylose isomerase (XI) is a multistep reaction that involves hydrogen transfer. We have determined the structure of this enzyme by neutron diffraction in order to locate H atoms (or their isotope D). Two studies are presented, one of XI containing cadmium and cyclic D-glucose (before sugar ring opening has occurred), and the other containing nickel and linear D-glucose (after ring opening has occurred but before isomerization). Previously we reported the neutron structures of ligand-free enzyme and enzyme with bound product. The data show that His54 is doubly protonated on the ring N in all four structures. Lys289 is neutral before ring opening and gains a proton after this; the catalytic metal-bound water is deprotonated to hydroxyl during isomerization and O5 is deprotonated. These results lead to new suggestions as to how changes might take place over the course of the reaction.

Abstract:

We have used inelastic neutron scattering and muon-spin rotation to compare the low energy magnetic excitations in single crystals of superconducting Fe(1.01)Se(0.50)Te(0.50) and non-superconducting Fe(1.10)Se(0.25)Te(0.75). We confirm the existence of a spin resonance in the superconducting phase of Fe(1.01)Se(0.50)Te(0.50), at an energy of 7 meV and a wavevector of (1/2, 1/2, 0). The non-superconducting sample exhibits two incommensurate magnetic excitations at (1/2, 1/2, 0) ± (0.18, - 0.18, 0) which rise steeply in energy, but no resonance is observed at low energies. A strongly dispersive low energy magnetic excitation is also observed in Fe(1.10)Se(0.25)Te(0.75) close to the commensurate antiferromagnetic ordering wavevector (1/2 - δ, 0, 1/2), where δ≈0.03. The magnetic correlations in both samples are found to be quasi-two-dimensional in character and persist well above the magnetic (Fe(1.10)Se(0.25)Te(0.75)) and superconducting (Fe(1.01)Se(0.50)Te(0.50)) transition temperatures.