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Hyperfine and Quadrupolar Interactions in Vanadyl Proteins and Model Complexes: Theory and Experiment

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Metals in Biology

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 29))

Abstract

The oxycation VO2+ has been employed for many years as an EPR spin probe of the metal binding sites in proteins. Its utility in these investigations has increased markedly with the advent and widespread use of high-resolution techniques such as ENDOR, ESEEM, and HYSCORE to measure isotropic and dipolar components of ligand hyperfine couplings. Measurements with model complexes in conjunction with DFT calculations have provided new insights into the dependence of g-factors and ligand and 51V nuclear hyperfine couplings on the electronic structure and coordination geometries of VO2+ chelates. These studies have greatly enhanced the information that can be derived from data with proteins. In the past fifteen years, highresolution techniques have been applied to a variety of VO2+- containing proteins and tissues samples, a number of which are reviewed here.

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Correspondence to N. Dennis Chasteen .

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Larsen, S.C., Chasteen, N.D. (2010). Hyperfine and Quadrupolar Interactions in Vanadyl Proteins and Model Complexes: Theory and Experiment. In: Hanson, G., Berliner, L. (eds) Metals in Biology. Biological Magnetic Resonance, vol 29. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-1139-1_11

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