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.

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.

Molecules that exhibit slow magnetic relaxation upon removal from a polarizing magnetic field are referred to as single-molecule magnets (SMMs). SMMs receive considerable attention owing to their potential utility in applications such as spin-based information storage. In these systems, the slow relaxation normally arises from the action of an easy-axis magnetic anisotropy, quantified by a negative axial zero-field splitting parameter, D < 0, on a high-spin ground state. Two separate EPR studies carried out in the DC field facility by users from UC Berkeley (chemistry) have identified compounds that undergo slow relaxation, even though the relevant magnetic ions possess easy-plane-type anisotropy (i.e. D > 0).

Hill, originally from outside Oxford, England, talks about the path to a career in science and how he ended up at the helm of a program that had helped to shape his own career.

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