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Home > L'ACCADEMIA > Maurizio Brunori

Maurizio Brunori

Eʹ Presidente della Classe di Scienze Fisiche, Matematiche e Naturali e Vice Presidente dellʹAccademia Nazionale dei Lincei.
Department of Biochemical Sciences
Sapienza - University of Rome
P.le Aldo Moro 5, 00185 Rome
Tel. +39-06-4450291 (University)
Fax: +39-06-49910717 (University)
Tel.: +39-06-6861159 (Lincei)
e-mail: maurizio.brunori@uniroma1.it

Vice President, Accademia Nazionale dei Lincei
Accademico Amministratore, Accademia Nazionale dei Lincei
Emeritus Professor, Sapienza - University of Rome
President of EMAN (Euro Mediterranean Academic Network)
President, Istituto Pasteur-Fondazione Cenci Bolognetti, Rome
Director, Centro Linceo Interdisciplinare “Beniamino Segre”, Accademia Nazionale dei Lincei
Director, Dept. of Biochemical Sciences "A. Rossi Fanelli", University of Rome "La Sapienza"
President, "Progetto Finalizzato Biotecnologie" of the National Research Council
Scientific Director, Istituto Pasteur-Fondazione Cenci Bolognetti, Rome
Member of the National Research Council Committee for Biology and Medicine
President of IUPAB (International Union of Pure and Applied Biophysics)
International Fogarty Scholar in Residence, NIH, Bethesda, MD, USA
Full Professor of Chemistry and Biochemistry, University of Rome "La Sapienza"
Full Professor of Molecular Biology, University of Camerino
Post-Doctoral Fellow, Urbana, IL, USA
Post-Doctoral Fellow, Goettingen, D
Docent in Biochemistry
University degree in Medicine at the University of Rome.


  • Member, Italian Society of Biochemistry and Molecular Biology (SIB)
  • Member, Italian Society of Biophysics and Molecular Biology (SIBBM)
  • Honorary Member, American Society for Biochemistry and Molecular Biology, USA
  • Member & Fellow, American Biophysical Society, USA
  • Member of EMBO, and of the Scientific Advisory Committee of EMBL
  • Member of the Accademia Nazionale dei Lincei (1987)
  • Premio Nazionale del Presidente della Repubblica (1985)
  • FEBS Lecturer (1989)
  • Member of the Academia Europaea (1998)
  • Officier de l’Ordre National du Mérite du Président de la République Française (2002)
  • Foreign Honorary Member, American Academy of Arts and Sciences (2006).
  • Member of the editorial board of Protein Sci. and Curr Opinion Structural Biology.


Maurizio Brunori established over the years many scientific collaborations with scientists from Italy and abroad on problems related to the structure-function relationships in proteins. Among the many, this is a selection:

  • A. Alfsen, CNRS, Faculté de Medicine, Paris (FR)
  • A. Ascenzi, Istituto di Anatomia Patologica, Università “La Sapienza”, Roma (IT).
  • P.A. Benedetti, Istituto di Biofisica del C.N.R., Pisa (IT).
  • M. Bolognesi, Dipartimento di Biochimica, Università di Milano (IT).
  • J. Bonaventura, Duke University Marine Laboratory, Beaufort, North Carolina (USA).
  • D. Bourgeois, Institut de Biologie Structurale, Grenoble (FR)
  • P. Brezinski, Department of Biochemistry, University of Stockholm (SW).
  • C. Cambillau, Centre du CNRS sur les Macromolécules Biologiques, Marseille (FR).
  • C.W. Canters, Department of Chemistry, University of Leiden, Leiden (NL).
  • P. Douzou, Institute de Biologie Physico-Chemique, Paris (FR).
  • W.A. Eaton, National Institutes of Health, Bethesda, MD (USA).
  • J. Engel, Department of Biophysical Chemistry, Biozentrum der Universität, Basel (CH).
  • Q.H. Gibson, Department of Biochemistry, Cornell University, Ithaca, NY (USA).
  • S.J. Gill, Department of Chemistry, University of Colorado, Boulder, CO (USA).
  • C. Greenwood, Division of Biological Sciences, University of East Anglia, Norwich (UK)
  • G: La Mar, Department of Molecular Biology, University of California, Davis, CA (USA).
  • B.G. Malmstrom, Department of Biochemistry, Chalmers University, Goteborg (SW).
  • G.U. Nienhaus, Institute of Applied Physics, Karlsrhue (D)
  • M.F. Perutz, Lab Mol Biol, Medical Research Council, Cambridge (UK).
  • M. Pocchiari, Istituto Superiore della Sanità, Roma (IT).
  • J.F. Taylor, Faculty of Medicine, University of Louisville, Louisville, KY (USA).
  • T. Traylor, Department of Chemistry, University of Southern California, San Diego, CA (USA).
  • F. Trottein, Institut Pasteur, Lille (FR).
  • M. Vendruscolo, Dept Chemistry, University of Cambridge, Cambridge (UK)
  • G. Weber, Department of Biochemistry and Biophysics, University of Illinois, Urbana, IL (USA).
  • M.T. Wilson, Department of Chemistry and Biochemistry, University of Essex, Colchester (UK).
  • K.H. Winterhalter, Laboratorium für Biochemie, ETH, Zürich (CH).
  • K. Wütrich, Department of Molecular Biology, ETH, Zürich (CH).
  • J. Wyman, Istituto Regina Elena, Roma (IT).
  • T. Yonetani, Department of Biophysics, University of Pennsylvania, Philadelphia, PE (USA).


The general field of interest is protein science, and the relationships between structure, function, folding and evolution of proteins, with attention for metalloproteins involved in the transport and activation of molecular oxygen, electron transfer and energy transduction. Recently original contributions to the ps-ms structural dynamics of proteins by laser spectroscopy, site directed mutagenesis, and time resolved Laue crystallography; and to the mechanism of protein folding/misfolding and their significance in the onset of neurodegenerative diseases. Scientific activity documented by more than 700 papers published in major Journals (Nature & Nat Struct Biol, PNAS, J. Biol. Chem, Biophys. J, J. Mol. Biol, FEBS Lett, FASEB J., JACS, EMBO J, etc.); Review articles (Ann. Rev. Biochem, Methods Enzymol, TIBS, Structure, etc.); and one book ("Hemoglobin and Myoglobin" 1971, North Holland).

SELECTED PUBLICATIONS (2001-2016) (out of over 700 papers published)

Brunori M. Nitric oxide, cytochrome-c oxidase and myoglobin. Trends Biochem. Sci. 26, 21-23, (2001).
Brunori M. and Gibson Q H. Cavities and packing defects in the structural dynamics of myoglobin. EMBO Rep. 2, 674-679, (2001).

Draghi F, Miele AE, Travaglini-Allocatelli C, Vallone B, Brunori M, Gibson QH and Olson J.S. Controlling ligand binding in myoglobin by mutagenesis. J. Biol. Chem. 277, 7509-7519, (2002).
Giuffrè A, Baroni MC, Brunori M, D'Itri E, Ludwig B, Malatesta F, Muller H-W and Sarti P. Nitric oxide reacts with the single-electron reduced active site of cytochrome c oxidase. J. Biol. Chem. 277, 22402-22406, (2002).

Bourgeois D, Vallone B, Schotte F, Arcovito A, Miele AE, Sciara G, Wulff M, Anfinrud P and Brunori M. Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography. Proc. Natl. Acad. Sci. USA. 100, 8704-8709, (2003).
Travaglini-Allocatelli C, Gianni S, Morea V, Tramontano A, Soulimane T and Brunori, M. Exploring the cytochrome c folding mechanism. J. Biol. Chem. 278, 41136-41140, (2003).

Vallone B, Nienhaus K, Matthes A, Brunori M and Nienhaus GU. The structure of carbonmonoxy neuroglobin reveals a heme-slinding mechanism for control of ligand affinity. Proc. Natl. Acad. Sci. USA. 101, 17351-17356, (2004).
Brunori M, Burgeois D and Vallone B. The structural dynamics of myoglobin. J. Struct. Biol. 147, 223-234, (2004).

Brunori M, Giuffrè A, Nienhaus K, Scandurra FM, Vallone B. Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes. Proc. Natl. Acad. Sci. USA. 102, 8483-8488, (2005).
Brunori M, Giuffrè A, Sarti P. Cytochrome c oxidase, ligands and electrons. J. Inorganic. Biochem. 99, 324-336, (2005).

Bourgeois D, Vallone B, Arcovito A, Sciara G, Schotte F, Anfinrud PA, and Brunori M. Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography. Proc. Natl. Acad. Sci. USA. 103, 4924-4929, (2006).
Brunori M, Vallone B. A globin for the brain. FASEB J. 20, 2192-2197, (2006).

Ivarsson Y, Travaglini-Allocatelli C, Jemth P, Malatesta F, Brunori M, Gianni S. An On-pathway Intermediate in the Folding of a PDZ Domain. J. Biol. Chem. 282, 8568-8572, (2007).
Brunori M, Vallone B. Neuroglobin, seven years after. Cell. Mol. Life Sci. 64, 1259-1268, (2007).

Ivarsson Y, Travaglini-Allocatelli C, Brunori M, Gianni S. Folding and mis-folding in a naturally occurring circularly permuted PDZ domain. J. Biol. Chem. 283, 8954-8960, (2008).
Giuffrè A, Moschetti T, Vallone B, Brunori M. Neuroglobin: Enzymatic reduction and oxygen affinity. Biochem. Biophys. Res. Commun. 367, 893-898, (2008).

Scaloni F, Gianni S, Federici L, Falini B, Brunori M. Folding mechanism of the C-terminal domain of nucleophosmin: residual structure in the denatured state and its pathophysiological significance. FASEB J. 23, 2360-2365, (2009).
Ivarsson Y, Travaglini-Allocatelli C, Brunori M, Gianni S. Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways. J. Am. Chem. Soc. 131, 11727-11733, (2009).

Brunori M. Myoglobin strikes back. Protein Sci. 19, 195-201, (2010).
Gianni S, Ivarsson Y, De Simone A, Travaglini-Allocatelli C, Brunori M, Vendruscolo M. Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain. Nat. Struct. Mol. Biol. 17, 1431-7, (2010).

Bellelli A, Brunori M. Hemoglobin allostery: Variations on the theme. Biochim. Biophys. Acta. 1807, 1262-72, (2011).
Gianni S, Haq SR, Montemiglio L, Jurgens MC, Engstrom A, Chi CN, Brunori M, Jemth P. Sequence specific long-range networks in PDZ domains tune their binding selectivity. J. Biol. Chem. 286, 27167-27175, (2011).

Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S. Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc. Natl. Acad. Sci. USA. 109, 17772-17776, (2012).
Levantino M, Spilotros A, Cammarata M, Schirò G, Ardiccioni C, Vallone B, Brunori M, Cupane A. The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin. Proc. Natl. Acad. Sci. USA. 109, 14894-14899, (2012). Brunori M. The Bohr effect before Perutz. Biochem. Mol. Biol. Educ. 40, 297-299, (2012).

Miele AE, Bellelli A, Brunori M. Hemoglobin Allostery: New Views on Old Players. J. Mol. Biol. 425, 1515-1526, (2013).
Giri R, Morrone A, Toto A, Brunori M, Gianni S. Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system. Proc. Natl. Acad. Sci. USA. 110, 14942-14947, (2013).

Brunori M. Variations on the theme: allosteric control in hemoglobin. FEBS. J. 281, 633-643, (2014).
Gianni S, Camilloni C, Giri R, Toto A, Bonetti D, Morrone A, Sormanni P, Brunori M, Vendruscolo M. Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein. Proc. Natl. Acad. Sci. USA. 111, 14141-14146 (2014)

Di Silvio E, Brunori M, Gianni S. Frustration Sculpts the Early Stages of Protein Folding. Angew Chem Int Ed 54, 10867-10869, (2015).
Brunori M, Miele AE. Hemoglobin. Encyclopedia Mol. Cell Biol. Mol. Medicine. Wyley VCH-Verlag GmbH. 1, 1-40 (2015)

Brunori M, Gianni S. Molecular Medicine: to be or not to be. Biophys. Chem. 214-215, 33-46, (2016).
Camilloni C, Bonetti D, Morrone A, Giri R, Dobson CM, Brunori M, Gianni S, Vendruscolo M. Towards a structural biology of the hydrophobic effect in protein folding. Sci. rep. 6, 28285, (2016).

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Palazzo Corsini - Via della Lungara, 10 - 00165 ROMA - tel. (39) 06 680271 - Fax (39) 06 6893616
E-mail: segreteria@lincei.it - Posta Elettronica Certificata