Synchrotron X-ray diffraction and absorption studies of CeM2X2 (M=Cu, Ni and X=Si, Ge) at high pressure

The equations of state of CeCu₂Si₂ and CeCu₂Ge₂ to about 60 GPa, as well as that of CeNi₂Ge₂ to 22 GPa and the valence state of Ce in CeCu₂Ge₂ to 20 GPa have been studied at room temperature in a diamond-anvil cell using synchrotron radiation sources. In each compound, the ambient-pressure phase (tetragonal ThCr₂Si₂-type structure) persisted to the highest pressure studied. The unit cell volumes of CeNi₂Ge₂ at ∼5 GPa and CeCu₂Ge₂ at ∼7 GPa, respectively, approached that of CeCu₂Si₂ taken at ambient pressure. From the equation-of-state data, the bulk modulus was derived to be 112.0±5.1 GPa for CeCu₂Si₂, 125.6±4.3 GPa for CeCu₂Ge₂, and 178.4±14.3 GPa for CeNi₂Ge₂. The valence state of Ce in CeCu₂Ge₂ remained trivalent throughout the pressure range investigated.     

Erratum to: Sources of 137Cs fluvial export from a forest catchment evaluated by stable carbon and nitrogen isotopic characterization of organic matter

Journal of Radioanalytical and Nuclear Chemistry -     

Sources of 137Cs fluvial export from a forest catchment evaluated by stable carbon and nitrogen isotopic characterization of organic matter

Fluvial export of particulate and dissolved ¹³⁷Cs was investigated to reveal its sources and transfer mechanisms in a broadleaved forest catchment using a continuous collection system. The finest size fraction (<75 µm), consisting of decomposed litter and surface mineral soil, was the dominant fraction in the particulate ¹³⁷Cs load, although the contribution of coarser size fractions increased during high water discharge in 2014. The dissolved ¹³⁷Cs originated from the decomposition of ¹³⁷Cs-contaminated litter. Temporal changes in ¹³⁷Cs distribution in the litter–mineral soil system indicated that the dissolved ¹³⁷Cs load will be moderated in several years, while particulate ¹³⁷Cs load has the potential to continue for a long time.

     

Ligand migration in myoglobin: a combined study of computer simulation and x-ray crystallography

A ligand-migration mechanism of myoglobin was studied by a multidisciplinary approach that used x-ray crystallography and molecular dynamics simulation. The former revealed the structural changes of the protein along with the ligand migration, and the latter provided the statistical ensemble of protein conformations around the thermal average. We developed a novel computational method, homogeneous ensemble displacement, and generated the conformational ensemble of ligand-detached species from that of ligand-bound species. The thermally averaged ligand-protein interaction was illustrated in terms of the potential of mean force. Although the structural changes were small, the presence of the ligand molecule in the protein matrix significantly affected the 3D scalar field of the potential of mean force, in accordance with the self-opening model proposed in the previous x-ray study.