Maurizio Brunori#

Brief curriculum
  • 2011 Emeritus Professor, Sapienza - University of Rome
  • 2010- President of EMAN (Euro Mediterranean Academic Network), Accademia dei Lincei
  • 2003-2007 President, Istituto Pasteur-Fondazione Cenci Bolognetti, Rome
  • 2001-2007 Director, Centro Linceo Interdisciplinare “Beniamino Segre”, Accademia Nazionale dei Lincei
  • 1998-2003 Director, Dept. of Biochemical Sciences "A. Rossi Fanelli", University of Rome "La Sapienza"
  • 1997-2002 President, "Progetto Finalizzato Biotecnologie" of the National Research Council
  • 1994-2001 Scientific Director, Istituto Pasteur-Fondazione Cenci Bolognetti, Rome
  • 1994-1998 Member of the National Research Council Committee for Biology and Medicine
  • 1990-1993 President of IUPAB (International Union of Pure and Applied Biophysics)
  • 1986/88/90 International Fogarty Scholar in Residence, NIH, Bethesda, MD, USA
  • 1974-2010 Full Professor of Chemistry and Biochemistry, University of Rome "La Sapienza"
  • 1972-1974 Full Professor of Molecular Biology, University of Camerino
  • 1968 Post-Doctoral Fellow, Urbana, IL, USA
  • 1966 Post-Doctoral Fellow, Goettingen, D
  • 1965 Docent in Biochemistry
  • 1961 University degree in Medicine at the University of Rome.

Memberships and honours
  • Member of the Italian Society of Biochemistry and Molecular Biology(SIB)
  • Member of the Italian Society of Biophysics and Molecular Biology (SIBBM)
  • Honorary Member of the American Society for Biochemistry and Molecular Biology, USA
  • Fellow of the American Biophysical Society, USA
  • Member of EMBO, and of SAC of EMBL (European Molecular Biology Lab., Heidelberg, D)
  • Member of the Accademia Nazionale dei Lincei
  • Premio Nazionale del Presidente della Repubblica (1985)
  • FEBS Lecturer (1989)
  • President (1990-93) of IUPAB (International Union of Pure and Applied Biophysics)
  • Member of the Academia Europaea (1996)
  • Officier de l’Ordre National du Mérite du Président de la République Française (2002)
  • Foreign Honorary Member of the American Academy of Arts and Sciences (2006).

Research interests

Main research interest is the study of the structure, function, folding and evolution of proteins, with particular attention for metalloproteins involved in the transport and activation of molecular oxygen, in electron transfer and in energy transduction. Over the last period, original contributions to the structural dynamics of proteins by time resolved spectroscopy, site directed mutagenesis, Laue crystallography; and mechanism of protein folding and misfolding.

Publications in the areas of rapid reaction techniques, spectroscopy of macromolecules, biochemical modifications, thermodynamics and structural biology of proteins.

Scientific activity documented by more than 600 papers published in major Journals (Nature, PNAS, J. Biol. Chem, Biophys. J, J. Mol. Biol, FEBS Lett, FASEB J., etc.), one book ("Hemoglobin and Myoglobin" 1971, North Holland), and several Review articles (Ann. Rev. Biochem, Methods Enzymol, TIBS ...).


"Myoglobin is the hydrogen atom and hemoglobin the hydrogen molecule of Molecular Biology", Perutz remarked many years ago. Nowadays in the era of proteomics, these two hemeproteins (and all variations on the theme) keep their role as paradigmatic models for our understanding of the function, evolution and structural dynamics of proteins at large. This is the area of protein science where Brunori is recognized as a world leader, with a consistent and remarkable set of discoveries over the last five decades. His recent successful work on neuroglobin shows, once more, the value of understanding in depth the biophysics, biochemistry and cell biology of hemeproteins. Brunori acquired international reputation for his early work on hemoglobin and myoglobin. His seminal contributions led to the conception and publication of a book, a classic in the field still used worldwide, that laid the foundation for our current understanding of the mechanism of cooperativity in hemoglobin (Antonini and Brunori, Hemoglobin and myoglobin, 1). The molecular basis of physiological adaptation for oxygen delivery under different stress conditions and the selective advantage of expressing different hemoglobins led to the proposal (with M.F. Perutz) of a structural interpretation of the peculiar properties of fish hemoglobins consistent with the two-state allosteric model (2,3). He provided the first evidence that the central exon of the myoglobin gene codes for a functionally competent domain, by preparing and characterizing mini-myoglobin (4), that he showed to be an autonomous folding unit. His attention for biomedicine inspired his science throughout, as demonstrated also by his most recent work on neuroglobin (5) proposing a mechanism to unveil the role of this recently discovered brain globin in neuroprotection and recovery from stroke.

Work in a related but distinct area dealt with electron transfer metalloproteins and energy transduction, with original discoveries on the structure and function of the mitochondrial enzyme cytochrome-c-oxidase, investigated by transient spectroscopy. Brunori's contribution to bioenergetics started with a lucid paper reporting, for the first time, direct kinetic evidence for multielectron steps in the reduction of dioxygen by cytochrome oxidase (6); and continued with the discovery of an activated state of the enzyme called pulsed oxidase (7) and the synchrony between electron transfer and proton pumping (8). These early findings helped rationalize a bunch of published data, and nowadays bear significance for the proton-pumping mechanism of the enzyme. While studying the mechanism of inhibition of cell respiration by nitric oxide (9), he demonstrated for the first time that some prokaryotic oxidases are endowed with a “vestigial” NO-reductase activity (10), an original experimental evidence that oxidases evolved from prokaryotic NO-reductases. His work on the reactions of cytochrome-c-oxidase with NO demonstrated that inhibition of the enzyme proceeds via two different pathways, a finding which paved the way to present understanding of the role of NO in the control of cellular respiration and mitochondrial physiology.

Over the last 15 years, Brunori's curiosity was attracted primarily by the structural dynamics of proteins. He has been a major contributor (with the group in Grenoble) to the emerging field of structural dynamics of proteins followed by time-resolved Laue crystallography; these studies (11,12) have led to a remarkable “movie” of protein relaxation from picosec to millisec, showing that the conformational relaxation of the globin follows an extended time course as evidence for a complex energy landscape and highlighting the hitherto unexpected role of internal cavities and packing defects in controlling function and reactivity (13). Brunori's interest in protein dynamics extended to folding mechanisms studied by kinetics, structure and site directed mutagenesis. His earlier work on the role of a common intermediate in the folding of all members of the cytochrome c family (14), was followed by extensive and revealing results on the folding of the small recognition domains called PDZ. This work culminated with proposal of a unifying mechanism for the folding of small globular proteins (15), and the significance of sequence permutation in controlling the population of a misfolded intermediate (16,17). The very recent discovery (18) that the denatured state of nucleophosmin is partially structured unveiled an unexpected feature relevant to the abnormal localization of its pathological mutants involved in the onset of acute myeloid leukemia, thereby suggesting novel therapeutic approaches.

Brunori’s impressive research accomplishments and broad scientific knowledge have propelled him into a position of scientific leadership which has been, and still is, instrumental in promoting high-quality biomedical science.

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