Abstract
Transition metal (d-group) ions are widespread in nature, essential for structural characteristics and mechanistic specificity of many proteins. Iron and copper are the two most prevalent metals in proteins responsible for the storage and transport of molecules, ions, and electrons. Electron paramagnetic resonance (EPR) spectroscopy has been extensively used for the determination of these metal ions without extensive disruption of the native protein moiety. It also detects variations in coordination geometry due to ligand substitutions as well as multiple valencies of the same metal. This review highlights the unique application of EPR spectroscopy to the study of iron and copper in biological systems. Mention is made of a select number of other metalloproteins.
Highlights
In this overview, the way in which Electron paramagnetic resonance (EPR) spectroscopy has been of use in the study of selected metalloproteins is presented
The way in which EPR spectroscopy has been of use in the study of selected metalloproteins is presented
Since ligands form basis of coordination geometry, hydrated ions are symmetric by default while protein-bound metals have variable symmetries
Summary
The way in which EPR spectroscopy has been of use in the study of selected metalloproteins is presented. Spectroscopic signatures of the metal ions would depend on types and numbers of ligands attached even if their oxidation states remain the same. These species are distinguishable by EPR spectroscopy through interaction of electron spin and their different orbital arrangements. The EPR spectroscopic act rests essentially on the energy difference, ∆E, between the two possible spin states Ms = +1/2 and Ms = −1/2 of an electron when an external magnetic field is applied. F.A. Taiwo / Electron paramagnetic resonance spectroscopic studies of iron and copper proteins in mutually opposite spins. The g-value is a measure of electronic interaction between the unpaired electron and the applied magnetic field. Further treatment of theory of EPR spectroscopy can be found in the literature [1,2]
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