The tradition of biological inorganic chemistry in Florence began in 1974 after
Ivano Bertini visited Harry B. Gray at Caltech. The biophysical characterization of metalloproteins had always included magnetic resonance investigation. Together with coworker Andrea Scozzafava and then-student Claudio Luchinat, Ivano Bertini began a series of spectroscopic studies on cobalt substituted carbonic anhydrase and other zinc enzymes with NMR. The interests of the group later broadened to include CuZnSOD, FeS proteins, hemoproteins, blue copper proteins, hydroxylating dioxygenases and ring opening dioxygenases.
In 1977, the laboratory began to use variable field nuclear relaxation studies to understand electron and nuclear spin relaxation, and to extract structural information from investigated systems.
In 1989, the lab acquired a 600 MHz NMR spectrometer, the largest magnetic field available at the time. This instrument was housed in a former church near the Chemistry Department of the University of Florence, in the downtown area. This device allowed the lab to make great strides in the development of experiments for the investigation of paramagnetic metalloproteins.
In 1994, the first solution structure of a paramagnetic protein was published. Since 1994 the lab has received funding for transnational access from the European Commission.
In 1996, the lab secured an 800 MHz spectrometer, the 3rd of its kind in the world. The space required for this instrument necessitated its installation at the new Polo Scientifico Scientific Campus of the University of Florence. In 1999, the Magnetic Resonance Center (CERM) building was constructed at the Polo Scientifico.
In 2003, the building was expanded to its present size, and a 900 MHz spectrometer was acquired.
In 2007, a solid-state 800 MHz spectrometer became the latest addition to the array of instruments in the lab.
