Laboratory of Bioinorganic Chemistry. Coordinator: Ciurli

Fig.1: Examples of proteins studied in the Laboratory of Bioinorganic Chemistry and some of the techniques used.

Research Themes

1. The study of the structure and chemistry of urease, an enzyme containing nickel that catalyzes the hydrolysis of urea to yield ammonium and bicarbonate ions in the last stage of organic nitrogen biomineralization. Urease inhibitors can increase the efficiency of nitrogen fertilization with urea and to decrease the negative effects of the infections of the gastrointestinal and urinary system by ureolytic pathogenic bacteria. The design of efficient inhibitors, and having minimal environmental and human impact, requires the molecular structure of the active site for the structure-based molecular design.
2. The study of the accessory proteins of urease, necessary for the transport of Ni(II) (UreE) and for the in vivo assembly of the metal site (UreD, UreF, UreG) of urease is an important theme of our group, as it represents a new possibility of identifying new possible targets for drug design. The identification of the structure of these proteins and their interactions, in the presence and absence of Ni(II) and other cofactors, is necessary to understand their operating mechanism and therefore its modulation, possibly inhibiting it with specific molecules.
3. Nichel homeostasis in bacteria is studied on a transcriptional level, through the determination of the structure-functions relationships of transcriptional metal dependent regulators (NikR, RcnR, SrnR) and of Ni(II) membrane transporters (NixA).
4.  Nickel is a Class 1 carcinogen in nasal and lung tissues and is an important environmental pollutant, found in fine powders resulting from air pollution. The molecular mechanisms underlying its carcinogenicity are still unknown. Through the study of nickel-binding proteins involved in lung tumor development, such as NDRG1, we seek to understand how nickel acts at the cellular level to induce cell transformation. This understanding is crucial for designing molecules that can prevent or treat this type of tumor.
5. Recently, we started a collaboration with scientists at Rensselaer Polytecnical Institute (Troy, NY, USA) with the aim of developing drugs capable of inhibiting the two proteases responsible for the virulence of Coronavirus, ad in particular SARS-CoV-2.

For additional information, visit our website.

Lab Members

Stefano Ciurli,  Full Professor

Francesco Musiani,  Associate Professor

Barbara Zambelli,  Associate Professor

Luca Mazzei,  Junior Assistant Professor

Arundhati Paul,  Research fellow

Simone Albani, Research fellow

Laura Rigobello, PhD Student

Giorgia Frumenzio, PhD Student

Claudio Pino, PhD Student

Noemi Carosella, PhD Student

Job Openings or Internship Projects

Please visit Prof. Stefano Ciurli,  Francesco Musiani, Barbara Zambelli personal website and our group website .

Main publications

• Zambelli, P. Basak, H. Hu, M. Piccioli, F. Musiani, V. Broll, L. Imbert, J. Boisbouvier, M.J. Maroney and S. Ciurli "The structure of the high-affinity nickel-binding site in the Ni,Zn-HypA•UreE₂ complex" Metallomics (2023) 15:mfad003
• Beniamino, V. Cenni, M. Piccioli, S. Ciurli, B. Zambelli “The Ni(II)-binding activity of the intrinsically disordered region of human NDRG1, a protein involved in cancer development” (2022) Biomolecules 12(9):1272.
• Camporesi, A. Minzoni, L. Morasso, S. Ciurli and F. Musiani "Nickel import and export in the human pathogen Helicobacter pylori, perspectives from molecular modelling" Metallomics (2021) 13:mfab066
• Masetti, M. Bertazzo, M. Recanatini, S. Ciurli and F. Musiani "Probing the transport of Ni(II) ions through the internal tunnels of the Helicobacter pylori UreDFG multimeric protein complex" J. Inorg. Biochem. (2021) 223:111554
• Mazzei, M. Cianci, S. Benini and S. Ciurli "The structure of the elusive urease-urea complex unveils the mechanism of a paradigmatic nickel-dependent enzyme" Angew. Chem. Int. Ed. (2019) 131:7493-7497