Contribution of Mössbauer spectroscopy to the investigation of Fe/S biogenesis

Abstract

Fe/S cluster biogenesis involves a complex machinery comprising several mitochondrial and cytosolic proteins. Fe/S cluster biosynthesis is closely intertwined with iron trafficking in the cell. Defects in Fe/S cluster elaboration result in severe diseases such as Friedreich ataxia. Deciphering this machinery is a challenge for the scientific community. Because iron is a key player, 57Fe-Mössbauer spectroscopy is especially appropriate for the characterization of Fe species and monitoring the iron distribution. This minireview intends to illustrate how Mössbauer spectroscopy contributes to unravel steps in Fe/S cluster biogenesis. Studies were performed on isolated proteins that may be present in multiple protein complexes. Since a few decades, Mössbauer spectroscopy was also performed on whole cells or on isolated compartments such as mitochondria and vacuoles, affording an overview of the iron trafficking.Graphical abstractThis minireview aims at presenting selected applications of 57Fe-Mössbauer spectroscopy to Fe/S cluster biogenesis

Methods to identify and characterize iron–sulfur oligopeptides in water

“…Similarly, the effect of temperature on the signals of CW spectra can help determine the contributions of each iron-sulfur cluster in solution. For example, overlapped peaks of [4Fe-4S] + and [2Fe-2S] + clusters may be disentangled by experiments that reveal the progressive loss in intensity of one component, i.e., that of the [4Fe-4S] + cluster, with increasing temperature until ultimately leaving spectra solely consisting of the [2Fe-2S] + component, which remains unaffected by temperature until approximately 70 K. 23,126 Mössbauer spectroscopy Mössbauer spectroscopy is extremely useful in characterizing iron-sulfur clusters. This technique can identify every type of iron-sulfur cluster and every iron centre present within the sample in a way that reveals their spin state, oxidation state, and electronic structure and gives insight into the coordination sphere (Fig.…”

PRE‐driven protein NMR structures: an alternative approach in highly paramagnetic systems

“…Its 3D structure is unknown, but homology modeling with other HiPIPs suggests that the protein has a compact globular structure, characterized by the absence of topologically relevant secondary structure elements; it is instead predicted to be composed essentially by a series of loops and turns wrapped around the [4Fe-4S] cluster [78,79]. The electronic properties of [Fe 4 S 4 ] 2+ in HiPIPs have been studied in detail over the past 40 years [3,[80][81][82][83][84][85][86][87][88]. The magnetic coupling within the [4Fe-4S] cluster makes the electronic correlation times of the individual iron ions much shorter than isolated high spin Fe 3+ or Fe 2+ ion; nevertheless, paramagnetic contributions to nuclear relaxation are significant for nuclei within a 10Å sphere from the cluster [89,90].…”

UVA irradiation increases ferrous iron release from human skin fibroblast and endothelial cell ferritin: Consequences for cell senescence and aging

“…Mossbauer spectroscopic studies, which do not depend on chelators to report iron concentrations, suggest that much of the mitochondrial iron exists as low mass Fe(III) complexes that are precursors for Fe/S cluster formation [74,75,78,79]. Thus, UV irradiation could lead to an acute increase in mitochondrial Fe(II) as a result of reduction of Fe(III)/S clusters to Fe(II) and consequent electron leakage from mitochondrial complex II [80].…”