Magnetic circular dichroism of 3d5/2 --> 2p3/2 resonant inelastic X-ray scattering at the Ho L(III)-edge in Ho3Fe5O12.

Magnetic Circular Dichroism (MCD) of Resonant Inelastic X-ray Scattering (RIXS) of 3d(5/2) --> 2p(3/2) decay (Ho Lalpha1) was measured at the Ho L(III)-edge in Ho3Fe5O12. The MCD-RIXS, in which the intermediate state has the 2p4f(n+1) configuration due to the quadrupolar transition of 2p --> 4f, was also observed at the pre-edge region of the Ho L(III)-edge. The obvious superposition of two peaks, which comes from the high-energy off-resonant Raman scattering and the fluorescence, could be found in both the RIXS and the MCD-RIXS when the energy of the incoming X-ray was 7eV higher than the white line.

Resonant X-ray emission spectra of K2Ni(CN)4 x H2O at the Ni K-edge.

Resonant X-ray emission spectra were measured at the Ni K-edge for a planar low-spin nickel complex K2Ni(CN)4 x H2O. In the Ni Kbeta emission spectra, a resonant X-ray Raman scattering was observed in the pre-edge region, showing linear energy dispersion of the emitted photon with the incident photon energy. No energy loss features corresponding to the ligand-to-metal charge-transfer (LMCT) was identified.

Physics in muscle research.

Muscle is one of few organs whose performance can be measured by physical quantities. However, very few attempts have been made to apply theoretical physics to muscle. In this paper we will see how physical principles can be applied by taking advantage of unique properties of muscle structure.

Collagenase degrades collagen in vivo in the ischemic heart.

Previously, we showed that ischemic rat heart contains an activated procollagenase capable of degrading collagen in vitro. We now demonstrate that the collagen resident in such hearts (in vivo) also becomes degraded, producing characteristic fragments implicating the action of an activated collagenase. The evidence is the appearance of amino-terminal dansyl-Ile (+dansyl-Leu) residues in pepsin digests of re-oxygenated rat hearts and immunoblots showing 3/4 length (alphaA) fragments from type I collagen.