Advanced Spin Resonance Facility

NREL's Advanced Spin Resonance Facility (ASRF) includes two Bruker electron paramagnetic resonance (EPR) spectrometers equipped with multifrequency, continuous-wave, advanced pulsed, and on-demand cyrogenic capabilities.

In addition, the ASRF includes a variety of light sources and photoreactors for performing temperature-controlled and in-situ illumination experiments.

EPR is a fundamental approach for understanding the role of electron spin in the mechanisms of enzymes and materials. The technique is able to probe subatomic, electronic, magnetic properties and electron-nuclear interactions of biological and chemical materials relevant to catalysis, energy transfer, and conversion. By applying EPR to a diverse set of biological enzymes, we are learning how complex electron transport is conducted across large spatial and temporal scales and coordinated with catalytic sites.

Our research in this area is leading to new understanding for how fundamental properties and complex phenomena of redox chains, such as spin-spin interactions occurring between iron-sulfur clusters, function in the mechanisms of electron transfer and catalysis. It is also leading to new understanding for how electrons are converted to high-value products in photochemical reactions by nanocrystal-enzyme biohybrids.

The resources of the ASRF are enabling researchers to elucidate new insights on the overarching function of spin properties in biological energy transformation processes. It also is paving the way for future advancement of more specialized approaches in partnership with other institutions, such as multifrequency EPR approaches with the National High Magnetic Field Laboratory. These types of experiments and ensuing simulations provide increased resolution of the electronic structure information contained within EPR spectra and enable more in-depth analysis of complex data inherent to biological systems.

Publications

Properties of the Iron-Sulfur Cluster Electron Transfer Relay in an [FeFe]-hydrogenase That Is Tuned for H₂ Oxidation Catalysis, Journal of Biological Chemistry (2024)

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