Darío A. Estrin

Darío A. Estrin is a gifted Argentine chemist. He received a M.Sc. (1985) from the University of Buenos Aires and a Ph.D. (1989) from the University of La Plata; he spent the two subsequent years as a postdoctoral research Fellow at Ohio State University. On completion of that Fellowship, he joined the Center for Research and Development in Sardinia, Cagliari, Italy, as a Senior Researcher (1992-94) before returning to Argentina to take up an appointment with CONICET as an Assistant Researcher; he became a Principal Researcher in 2006. In 1996, concurrent with his work at CONICET, he joined the University of Buenos Aires as the Head of its Molecular Modeling Laboratory, and was appointed an Assistant Professor of chemistry the following year; he is currently an Associate Professor.

Mr. Estrin has been an invited lecturer at many renowned institutions, including the University of Genova, Italy; Queen’s University of Belfast; the Institute for Interdisciplinary Applications in Physics, Palermo, Italy; the Free University, Berlin; and the University Louis Pasteur, Strasbourg, France. In 2002, he was the IBM Lowdin Fellow. From 1998 to 2005, he was an associate member of UNESCO’s International Center for Theoretical Physics. Among his awards are the Physical Chemistry Young Investigator Award from the Argentine National Academy of Sciences (2001) and the Bernardo Houssay Prize, from the Science and Technology Ministry of Buenos Aires (2002).

During his Guggenheim Fellowship term, Darío Estrin worked on  computer simulations of hemeproteins of physiopathological relevance. The main goals of the project involve the application of quantum-classical (QM-MM) and purely classical schemes to obtain information about the structural properties and reactivity of selected heme proteins. Specifically, we have studied (i) the physiological role of recently discovered hexa coordinated globins, (ii) the possible vasoactive effects of deoxyhemoglobin via nitrite reduction to nitric oxide, (iii) the nitric oxide binding mechanism in nitrophorin 4, a protein  related to Chagas’s disease, and (iv) ligand binding and reactivity of  bacterial truncated hemoglobins.