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Low Frequency EPR of Cu2+ in Proteins

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Biomedical EPR, Part A: Free Radicals, Metals, Medicine, and Physiology

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 23))

Abstract

Frequencies lower than X-band give better-resolved CW EPR spectra for copper(II) complexes. Use of S-band (2-4 GHz) revealed a new type of copper center in proteins. In the g|| region of the spectrum there is narrowing of the linewidths for negative values of mI with minimum linewidths near 3 GHz. Examples of S-band spectra are given for particulate methane monooxygenase, Cu-substituted prions, azurin, laccase, mixed valence dinuclear copper sites in nitrous oxide reductase and Cytochrome c oxidase, and from Cu in clusters.

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  1. National Biomedical ESR Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI, 53226

    William E. Antholine

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  1. University of Denver, Denver, Colorado

    Sandra R. Eaton , Gareth R. Eaton  & Lawrence J. Berliner ,  & 

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Antholine, W.E. (2005). Low Frequency EPR of Cu2+ in Proteins. In: Eaton, S.R., Eaton, G.R., Berliner, L.J. (eds) Biomedical EPR, Part A: Free Radicals, Metals, Medicine, and Physiology. Biological Magnetic Resonance, vol 23. Springer, Boston, MA. https://doi.org/10.1007/0-387-26741-7_14

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