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Characterization of Paramagnetic Iron-Sulfur Clusters Using Electron Paramagnetic Resonance Spectroscopy

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Fe-S Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2353))

Abstract

Continuous-wave (CW) electron paramagnetic resonance (EPR) spectroscopy is a powerful ally in characterizing the multitude of redox-active iron-sulfur cluster-containing ([Fe-S]) species present in biological samples. The technique detects only those clusters that are paramagnetic—having a nonzero total electron spin (S > 0)—thus, it can discriminate between clusters in different oxidation states. The low-temperature CW-EPR spectrum of an [Fe-S] yields the three magnetic g-values that serve as a fingerprint of its electronic structure. This chapter briefly describes the underlying theory that defines this electronic structure and provides a recipe for the acquisition and analysis of EPR spectra of [Fe-S] proteins.

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Authors and Affiliations

  1. Department of Chemistry, Wake Forest University, Winston-Salem, NC, USA

    Troy A. Stich

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  1. Troy A. Stich
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Correspondence to Troy A. Stich .

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  1. Department of Chemistry, Wake Forest University, Winston Salem, NC, USA

    Patricia C. Dos Santos

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Stich, T.A. (2021). Characterization of Paramagnetic Iron-Sulfur Clusters Using Electron Paramagnetic Resonance Spectroscopy. In: Dos Santos, P.C. (eds) Fe-S Proteins. Methods in Molecular Biology, vol 2353. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1605-5_14

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  • DOI: https://doi.org/10.1007/978-1-0716-1605-5_14

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1604-8

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