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Nitroxide Spin-Labelling and Its Role in Elucidating Cuproprotein Structure and Function.

Authors
  • Jones, Christopher E1
  • Berliner, Lawrence J2
  • 1 The School of Science and Health, Western Sydney University, Locked Bag 1797, Penrith, NSW, 2759, Australia. [email protected] , (Australia)
  • 2 Department of Chemistry and Biochemistry, University of Denver, Denver, CO, 80208-0183, USA.
Type
Published Article
Journal
Cell Biochemistry and Biophysics
Publisher
Springer-Verlag
Publication Date
June 2017
Volume
75
Issue
2
Pages
195–202
Identifiers
DOI: 10.1007/s12013-016-0751-8
PMID: 27342129
Source
Medline
Keywords
License
Unknown

Abstract

Copper is one of the most abundant biological metals, and its chemical properties mean that organisms need sophisticated and multilayer mechanisms in place to maintain homoeostasis and avoid deleterious effects. Studying copper proteins requires multiple techniques, but electron paramagnetic resonance (EPR) plays a key role in understanding Cu(II) sites in proteins. When spin-labels such as aminoxyl radicals (commonly referred to as nitroxides) are introduced, then EPR becomes a powerful technique to monitor not only the coordination environment, but also to obtain structural information that is often not readily available from other techniques. This information can contribute to explaining how cuproproteins fold and misfold. The theory and practice of EPR can be daunting to the non-expert; therefore, in this mini review, we explore how nitroxide spin-labelling can be used to help the inorganic biochemist gain greater understanding of cuproprotein structure and function in vitro and how EPR imaging may help improve understanding of copper homoeostasis in vivo.

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