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Article Dans Une Revue Angewandte Chemie International Edition Année : 2021

In cellulo Mossbauer and EPR studies bring new evidence to the long-standing debate on iron-sulfur cluster binding in human anamorsin

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Human anamorsin is an iron-sulfur (Fe-S)-cluster-binding protein acting as an electron donor in the early steps of cytosolic iron-sulfur protein biogenesis. Human anamorsin belongs to the eukaryotic CIAPIN1 protein family and contains two highly conserved cysteine-rich motifs, each binding an Fe-S cluster. In vitro works by various groups have provided rather controversial results for the type of Fe-S clusters bound to the CIAPIN1 proteins. In order to unravel the knot on this topic, we used an in cellulo approach combining Mossbauer and EPR spectroscopies to characterize the iron-sulfur-cluster-bound form of human anamorsin. We found that the protein binds two [2Fe-2S] clusters at both its cysteine-rich motifs.
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hal-03245170 , version 1 (18-11-2021)

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Sara Matteucci, Francesca Camponeschi, Martin Clémancey, Simone Ciofi-Baffoni, Geneviève Blondin, et al.. In cellulo Mossbauer and EPR studies bring new evidence to the long-standing debate on iron-sulfur cluster binding in human anamorsin. Angewandte Chemie International Edition, 2021, 60 (27), pp.14841-14845. ⟨10.1002/anie.202102910⟩. ⟨hal-03245170⟩
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