Born on 6 December 1940, in Pisa, Italy, Ivano obtained a doctorate in chemistry cum laude at the University of Florence, in 1964. He stayed with his mentor Luigi Sacconi in Florence until 1975 when he was appointed full professor at the university. Immensely interested in the role of inorganic chemistry in biology, he felt that real progress on the most challenging problems could only be made after the development of powerful new biophysical methods for experimental investigations. His method of choice was NMR.

A visit to the ETH Zurich in 1965 culminated in Ivano's first NMR paper1. He subsequently worked with Bill Horrocks at Princeton University (1968–1969) on NMR of paramagnetic complexes. He began his work on metals in biology in 1974 during a very productive period of collaboration with one of us (H.B.G.). And shortly thereafter, in Florence, he cleverly employed paramagnetic metal-ion probes to elucidate the mechanisms of action of several zinc enzymes, including carbonic anhydrase, carboxypeptidase, alcohol dehydrogenase and superoxide dismutase. During this period, he developed a strong interest in both theoretical and experimental studies of nuclear and electron relaxation processes. He teamed up with IBM's Seymour Koenig, who had a homemade relaxometer for nuclear relaxation experiments at variable magnetic fields. Following his work with Koenig, in 1994, he determined the first NMR solution structure of a paramagnetic metalloprotein, the high-potential iron-sulfur protein I from Ectothiorhodospira halophila2. Over 160 protein structures have been solved in the lab in Florence since that landmark work was published. Thanks to his strong theoretical background in electron and nuclear relaxation, as well his knowledge of the physics that produces hyperfine shifts, he then developed protocols to solve challenging macromolecular structures, taking advantage of paramagnetic-based, nonconventional NMR restraints. Notably, these protocols have been incorporated into many widely used analysis programs.

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