News

In a recent publication from the Kauzlarich and Taufour labs (Devlin et. al., Chem. Mater., 2018) describes the synthesis, structure, and magnetic properties of a new layered Zintl phase and structure type, Eu₁₁Zn₄Sn₂As₁₂. Eu₁₁Zn₄Sn₂As₁₂ is made up of unique beehive Zn₄As₆ sheets with pseudo-trigonal planer Zn and ethane-like Sn₂As₆ units. Eu₁₁Zn₄Sn₂As₁₂ exhibits a large negative colossal magnetoresistance of 2690-fold at 9 T.

A recent publication from the David, Siegel and Lim (Academia Sinica, Taiwan) labs (Nuñez et al., JACS, 2018) provides insight into the coordination sphere and critical role of a Zn²⁺ metal binding site in the DNA repair glycosylase MUTYH. Genome database mining and sequence alignment of MUTYH orthologs, along with computational modeling, identified and supported Zn²⁺ ligation by four Cys residues. Three of the Cys residues lie in an interdomain connector region unique to mammalian MutY enzymes, while the 4th Cys is located in close proximity to the Fe-S cluster DNA binding domain.

In a recent publication (Su and coworkers, X-ray Mediated Release of Molecules and Engineered Proteins from the Surface of Nanoparticles, 2018) the Guo and Siegel Labs presents unprecedented efficient release of modified green fluorescent proteins (GFP) from the surface of silica-coated gold nanoparticles.

In a recent publication (Su and coworkers, X-ray Mediated Release of Molecules and Engineered Proteins from the Surface of Nanoparticles, 2018) the Guo and Siegel Labs presents unprecedented efficient release of modified green fluorescent proteins (GFP) from the surface of silica-coated gold nanoparticles.

In a recent publication (Jenkins et al. Ultrafast Spintronics: Dynamics of the Photoisomerization-Induced Spin–Charge Excited-State (PISCES) Mechanism in Spirooxazine-Based Photomagnetic Materials), the Larsen Lab, in collaboration with the Frank Lab (U. Victoria) explored the primary photodynamics of a novel Co coordination complex that via the structural evolution of a modified spirooxazine ligand will induced long living spin states.

In a recent publication in Angewandte Chemie, the Cramer group and collaborators use a synchrotron technique, NRVS, to probe the coupling between the hydrogenase H-cluster and its neighboring proton transfer chain. NRVS is a vibrational spectroscopy that is only sensitive to the motions of the resonant nucleus, in this case 57Fe vibrations.

In a recent publication (Farahvash and Stuchebrukhov, The Journal of Physical Chemistry: B, 2018) the Stuchebrukhov Lab use Dowser++ (a protein hydration program designed by the group) to illustrate that the mitochondrial enzyme cytochrome c oxidase (CcO) permits a significantly higher hydration state than is seen in x-ray crystal structures. Analyzing the dynamic nature of these waters with MD simulations leads to several interesting results.