2020
DOI: 10.3390/ijms21249619
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Effects of Fe2+/Fe3+ Binding to Human Frataxin and Its D122Y Variant, as Revealed by Site-Directed Spin Labeling (SDSL) EPR Complemented by Fluorescence and Circular Dichroism Spectroscopies

Abstract: Frataxin is a highly conserved protein whose deficiency results in the neurodegenerative disease Friederich’s ataxia. Frataxin’s actual physiological function has been debated for a long time without reaching a general agreement; however, it is commonly accepted that the protein is involved in the biosynthetic iron-sulphur cluster (ISC) machinery, and several authors have pointed out that it also participates in iron homeostasis. In this work, we use site-directed spin labeling coupled to electron paramagnetic… Show more

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Cited by 8 publications
(12 citation statements)
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“…The experiments with Fe 3+ were performed on the same solution as above with the addition of 1 μL of Fe 3+ stock solution. As previously verified [ 32 ], this volume of acidic iron solution does not change the pH of the solution.…”
Section: Methodssupporting
confidence: 78%
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“…The experiments with Fe 3+ were performed on the same solution as above with the addition of 1 μL of Fe 3+ stock solution. As previously verified [ 32 ], this volume of acidic iron solution does not change the pH of the solution.…”
Section: Methodssupporting
confidence: 78%
“…Human mitochondrial SOD (SOD2) was purchased as a His-tag recombinant protein from Technical Novusbio; the SOD2 buffer was Tris HCl buffer (20 mM, pH 8) containing 20% glycerol. The M-TETPO label was synthesized as previously described [ 32 ].…”
Section: Methodsmentioning
confidence: 99%
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“…Iron binding is also not exclusively localized to the α-helix 1 region; frataxin contains a pool of additional acidic ligands capable of participating in binding iron on the β-strands 1 and 2 [55]. Specifically, FXN D122Y mutation lowers the frataxin Fe(II)-binding affinity but does not impact NFS1 binding, so the potential role of this and additional acidic residues within the β-sheet region related to interacting with metal may be important during assembly [56,57]. Assuming frataxin iron binding is in part driven by availability of Fe(II) from the mitochondrial matrix free iron pool, the flexibility of these iron-binding sites provide for a dynamic interaction between protein binding partners in an iron-dependent manner.…”
Section: The Frataxin Proteinmentioning
confidence: 99%