Measurements performed in the EMR program demonstrate that the nuclear spins associated with donor states in silicon field-effect transistors can be polarized at high magnetic fields by controlling the current and gate voltage on the device, i.e., the nuclear polarization can be controlled purely by electrical means.

Dynamic nuclear polarization (DNP) coupled with solid state NMR can provide orders of magnitude enhancement to normally weak NMR signals, thereby enabling the study of inherently dilute proteins such as membrane proteins. Here we demonstrate a new approach to obtain DNP signal enhancements of membrane proteins by utilizing spin labeled lipids as the polarization agents. This strategy results in more than 2x in signal enhancements of a membrane protein when compared to standard DNP sample preparation techniques.

MagLab users have employed a combination of ab-initio theory and a newly developed high-pressure, high-field ferromagnetic resonance technique, which is uniquely sensitive to anisotropic magnetic interactions, to gain insights into the importance of spin-orbit coupling effects in a range of organic materials where this effect is usually considered to be small. The findings may be applicable to topics as diverse as spintronics and topological spin phases.

Square-planar high-spin Fe(II) molecular compounds are rare. Using an easily modifiable pincer-type ligand, the successful synthesis of the first compound of this type that breaks the FeO4 motif was achieved, and the first spectroscopic evidence that the geometry and spin state persist in solution was obtained.

Researchers from the National High Magnetic Field Laboratory user program performed high-frequency (329 GHz) electron magnetic resonance (EMR) experiments to address questions of fundamental importance in catalysis 1) improving industrial production of ammonia and ammonia-derived fertilizers, and 2) understanding of the atmospheric nitrogen cycle.

Research suggests that anisotropy in the high-symmetry coordination environment of Ni(II) complex is an order of magnitude larger than any previously known.

A lot of the research conducted in powerful magnets ends up having a powerful effect on our day-to-day lives.

Oxalate Decarboxylase (OxDC) is an enzyme that catalyzes the manganese-dependent breakdown of the oxalate monoanion into carbon dioxide and formate. EPR measurements performed at very high magnetic fields greatly simplify the task of assigning fine structure parameters to each of the Mn(II) centers in wild-type OxDC. The results provide new insights into the strengths and limitations of theoretical methods for understanding protein-bound Mn(II), setting the stage for future EPR studies of Mn(II) centers in OxDC.

This work defines a new mechanism for radical-mediated catalysis of a protein substrate, and has broad implications for applied biocatalysis and for understanding oxidative protein modification during oxidative stress.

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