Magnetic Resonance Center and Department of Chemistry

Via L. Sacconi 6
50019 Sesto Fiorentino, (FI) -Italy

Tel: +39 055 4574196
e-mail: camponeschi[at]

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Francesca Camponeschi graduated cum laude in Chemistry in 2007 at the University of Rome “Tor Vergata” and obtained her PhD in “Chemical Science” from the University of Siena in 2010, where she has been a post-doctoral fellow from 2011 to 2013. In 2014 she joined the Magnetic Resonance Center and the Interuniversitary Consortium for Magnetic Resonance of Metallo Proteins (CIRMMP) of the University of Florence as a post-doctoral fellow. The research activity of Francesca Camponeschi is mainly focused on the investigation at molecular level of the cellular mechanisms responsible for the biogenesis of iron-sulfur proteins in humans. Her studies involve the investigation at atomic level of the structural and spectroscopic properties of protein-metal cofactor and protein-protein complexes, through the use of an integrated structural biology approach, that involves both the expression and purification of recombinant proteins for structural studies, and their biophysical and biochemical characterization through solution NMR, EPR, UV-Visible and CD spectroscopies, and chromatographic techniques. She is currently working as RTDa Lecturer at the Department of Chemistry of the University of Florence.



Structural biology; molecular biology; solution NMR spectroscopy; EPR spectroscopy; metalloproteins; metal transport; iron-sulfur protein biogenesis; iron-sulfur clusters.



1) Bargagna B, Matteucci S, Ciofi-Baffoni S, Camponeschi F, Banci L., Unraveling the mechanism of [4Fe-4S] cluster assembly on the N-terminal cluster binding site of NUBP1. Protein Sci. (2023) 32:e4625.
2) Matteucci S, Camponeschi F, Clémancey M, Ciofi-Baffoni S, Blondin G, Banci L. In Cellulo Mössbauer and EPR Studies Bring New Evidence to the Long-Standing Debate on Iron-Sulfur Cluster Binding in Human Anamorsin. Angew Chem Int Ed Engl. (2021) 60, 14841-14845.
3) Camponeschi F, Prusty NR, Heider SAE, Ciofi-Baffoni S, Banci L. GLRX3 Acts as a [2Fe-2S] Cluster Chaperone in the Cytosolic Iron-Sulfur Assembly Machinery Transferring [2Fe-2S] Clusters to NUBP1. J Am Chem Soc. (2020) 142, 10794-10805.
4) Camponeschi F, Muzzioli R, Ciofi-Baffoni S, Piccioli M, Banci L. Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes. J Mol Biol. (2019) 431, 4514-4522.
5) Camponeschi F, Ciofi-Baffoni S, Banci L. Anamorsin/Ndor1 Complex Reduces [2Fe-2S]-MitoNEET via a Transient Protein-Protein Interaction. J Am Chem Soc. (2017) 139, 9479-9482.