Research Topics
Genomes and GenesSpecies | M BrunoriSummaryAffiliation: University of Rome La Sapienza Country: Italy Publications
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Detail Information
Publications
Structural dynamics of myoglobinM Brunori
Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, Italy
Biophys Chem 86:221-30. 2000..These results support the viewpoint that pre-existing 'packing defects' in the protein interior play a major role in controlling the dynamics of ligand binding, including oxygen, and thereby acquire a survival value...
The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobinM Brunori
Department of Biochemical Sciences, Consiglio Nazionale delle Ricerche Centre of Molecular Biology, University La Sapienza, 00185 Rome, Italy
Proc Natl Acad Sci U S A 97:2058-63. 2000....- The oxygen reactive species of cytochrome-c-oxidase: an alternative viewM Brunori
Department of Biochemical Sciences, University of Rome, La Sapienza, Italy
FEBS Lett 314:191-4. 1992.... - Control of electron transfer by the electrochemical potential gradient in cytochrome-c oxidase reconstituted into phospholipid vesiclesP Sarti
Department of Biochemical Sciences, University of Rome, La Sapienza, Italy
J Biol Chem 265:5554-60. 1990..Brunori, M., Sarti, P., Colosimo, A., Antonini, G., Malatesta, F., Jones, M.G., and Wilson, M.T. (1985) EMBO J. 4, 2365-2368), and their bioenergetic relevance is discussed with reference to the proton pumping activity of the enzyme... - Nitric oxide and cytochrome c oxidase: mechanisms of inhibition and NO degradationP Sarti
Department of Biochemical Sciences, University of Rome La Sapienza, Rome, Italy
Biochem Biophys Res Commun 274:183-7. 2000..When the reaction occurs with the oxidized binuclear site, light has no effect and NO is oxidized to harmless nitrite eventually released in the bulk, accounting for catalytic NO degradation... - Spectral analysis of cytochromes in rat heart myocytes: transient and steady-state photodiode array spectrophotometry measurementsP Sarti
Department of Biochemical Sciences, University of Rome La Sapienza, Italy
Arch Biochem Biophys 299:8-14. 1992..Spectral analysis was improved by adding carbon monoxide at concentrations which did not affect cytochrome c oxidase activity, but kept myoglobin fully saturated (and thus uninfluential to absorbance changes)... - Sulfolobus acidocaldarius terminal oxidase. A kinetic investigation and its structural interpretationA Giuffre
Department of Biochemical Sciences, University of Rome, La Sapienza, Italy
J Biol Chem 269:31006-11. 1994..On the contrary, a second CO binding site having unusual properties for aa3 terminal oxidases can be detected in the dithionite-reduced membranes... - Mutagenesis of nitrite reductase from Pseudomonas aeruginosa: tyrosine-10 in the c heme domain is not involved in catalysisF Cutruzzola
Dipartimento di Scienze Biochimiche A Rossi Fanelli and Centro di Biologia Molecolare del CNR, Universita di Roma La Sapienza, Italy
FEBS Lett 412:365-9. 1997.... - Nitric oxide and cellular respirationM Brunori
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Italy
Cell Mol Life Sci 56:549-57. 1999..Finally, since COX has been proposed to catalyze the degradation of NO into either nitrous oxide (N2O) or nitrite, we consider the putative role of this enzyme in the catabolism of NO in vivo... - Cavities and packing defects in the structural dynamics of myoglobinM Brunori
Istituto Pasteur Fondazione Cenci Bolognetti and Department of Biochemical Sciences A Rossi Fanelli, University of Rome La Sapienza, P le Aldo Moro 5, 00185 Rome, Italy
EMBO Rep 2:674-9. 2001..These results convey the general picture that pre-existing internal cavities are involved in controlling the dynamics and reactivity of the reactions of Mb with O2 and other ligands, including NO... - The structural dynamics of myoglobinM Brunori
Departimento di Scienze Biochimiche and Istituto Pasteur Fondazione Cenci Bolognetti, Universita di Roma La Sapienza, Rome, Italy
J Struct Biol 147:223-34. 2004..The extended relaxation of the globin moiety directly observed by Laue crystallography reflects re-equilibration among conformational substates known to play an essential role in controlling protein function... - The caa3 terminal oxidase of Bacillus stearothermophilus. Transient spectroscopy of electron transfer and ligand bindingA Giuffre
Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome La Sapienza, 00185 Rome, Italy
J Biol Chem 271:13987-92. 1996..The data from the reaction with O2 reveal a remarkable similarity in the kinetic, equilibrium, and optical properties of caa3 and the electrostatic complex cytochrome c/cytochrome c oxidase... - Control of heme reactivity by diffusion: structural basis and functional characterization in hemoglobin mutantsA E Miele
Department of Biochemical Sciences A. Rossi Fanelli and CNR Centre for Molecular Biology, University of Rome La Sapienza, P.le A. Moro 5, 00185 Rome, Italy
Biochemistry 40:14449-58. 2001.... - The unusual stability of saporin, a candidate for the synthesis of immunotoxinsS Santanché
Dipartimento di Scienze Biochimiche Alessandro Rossi Fanelli, Universita di Roma La Sapienza, Italy
Biochem Biophys Res Commun 234:129-32. 1997..The remarkable resistance of saporin to denaturation and proteolysis suggests this protein as an ideal candidate for biotechnological applications... 
Structural dynamics of myoglobinM Brunori
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Roma, Italy
Methods Enzymol 437:397-416. 2008..A synopsis of the more significant findings obtained by laser photolysis of myoglobin-CO crystals is also presented, emphasizing the more general aspects of dynamics relevant to the complex energy landscape of a protein...- Photochemically induced electron transferA Bellelli
Department of Biochemical Sciences, University of Rome La Sapienza, and CNR Center of Molecular Biology, P.le A. Moro, Rome, 00185, Italy
Methods 24:139-52. 2001.... - Refolding kinetics of cytochrome c(551) reveals a mechanistic difference between urea and guanidineS Gianni
Istituto Pasteur-Fondazione Cenci Bolognetti e Centro di Biologia Molecolare del CNR, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, , 00185 Rome, Italy
Protein Sci 10:1685-8. 2001..We propose, therefore, a simple kinetic test to obtain a mechanistic interpretation of nonlinear dependences of DeltaG(w) on GdnHCl concentration on the basis of kinetic refolding experiments in the presence of both denaturants... - N-oxide sensing and denitrification: the DNR transcription factorsS Rinaldo
Department of Biochemical Sciences A Rossi Fanelli and Istituto di Biologia e Patologia Molecolari CNR, University of Rome La Sapienza, P le A Moro 5, 00185 Rome, Italy
Biochem Soc Trans 34:185-7. 2006.... - Multiplicity of interactions between dromedary hemoglobin and solvent components. A structural and functional studyA Bertollini
Department of Biochemical Sciences, University of Rome La Sapienza, Italy
Eur J Biochem 176:669-73. 1988..In conclusion, the functional properties of dromedary hemoglobin do not depend in any simple way on the variety of stabilized conformations... - Nitric oxide, cytochrome-c oxidase and myoglobinM Brunori
Department of Biochemical Sciences, University of Rome La Sapienza, P le Aldo Moro 5, 00185, Rome, Italy
Trends Biochem Sci 26:21-3. 2001..Here, Maurizio Brunori argues that myoglobin can also play the role of intracellular scavenger of nitric oxide, an inhibitor of mitochondrial cytochrome-c oxidase, thereby protecting respiration in the skeletal muscle and the heart... - The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural propertiesF Cutruzzola
Dipartimento di Scienze Biochimiche A Rossi Fanelli and Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Universita di Roma La Sapienza, P le A Moro 5, 00185 Rome, Italy
Proc Natl Acad Sci U S A 98:2232-7. 2001..We conclude that the two invariant His play a crucial role in the activity and the structural organization of cd(1) nitrite reductase from P. aeruginosa... - Neuroglobin, seven years afterM Brunori
Istituto Pasteur Fondazione Cenci Bolognetti and Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Rome, Italy
Cell Mol Life Sci 64:1259-68. 2007..These features may pave the way to an understanding of neuroprotection by neuroglobin... - Trichomonas vaginalis degrades nitric oxide and expresses a flavorubredoxin-like protein: a new pathogenic mechanism?P Sarti
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy
Cell Mol Life Sci 61:618-23. 2004..vaginalis would appear relevant to both pathology and evolutionary biology. Interestingly, genomic analysis has recently demonstrated that Giardia intestinalis and other pathogenic protists have genes coding for ATFs... - N-oxide sensing in Pseudomonas aeruginosa: expression and preliminary characterization of DNR, an FNR-CRP type transcriptional regulatorS Rinaldo
Department of Biochemical Sciences 'A. Rossi Fanelli, University of Rome La Sapienza, P.le A. Moro 5, 00185 Rome, Italy
Biochem Soc Trans 33:184-6. 2005.... - A globin for the brainM Brunori
Istituto Pasteur Fondazione Cenci Bolognetti and Department of Biochemical Sciences, University of Rome La Sapienza, Rome, Italy
FASEB J 20:2192-7. 2006..Thus it appears that neuroglobin is a stress-responsive sensor for signal transduction in the brain, mediated by a ligand-linked conformational change of the protein... - N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosaD Nurizzo
Architecture et Fonction des Macromolecules Biologiques, U P R 9039 C N R S, I B S M, Marseille, France
Structure 5:1157-71. 1997..NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere... - [Possible effects of non invasive mechanical ventilation on respiratory drive and muscles]A Perrone
Servizio di Fisiopatologia Respiratoria, Dipartimento di Scienze Cardiovascolari e Respiratorie, Policlinico Umberto I, 00161 Roma, Italia
Clin Ter 158:11-6. 2007..To evaluate whether long-term Non-Invasive Mechanical Ventilation (NIMV) might have an effect on respiratory drive and respiratory muscles strength, measuring mouth occlusion pressure (P0,) and maximal inspiratory pressure (MIP)... - Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosaD Nurizzo
Architecture et Fonction des Macromolecules Biologiques, UPR 9039 CNRS, IBSM, Marseille, France
Biochemistry 37:13987-96. 1998.... - [Pulmonary physiopathology in scleroderma: study of respiratory function in 86 patients]A Perrone
UOC di Fisiopatologia e Riabilitazione Respiratoria, Dipartimento di Scienze Cardiovascolari e Respiratorie, Policlinico Umberto I, Roma, Italia
Clin Ter 158:115-20. 2007..To contribute to an early diagnosis of pulmonary involvement in scleroderma by evaluating the correlation between respiratory symptoms and functional respiratory data observed... - The anti-schistosomal drug praziquantel is an adenosine antagonistF Angelucci
Dipartimento di Scienze Biochimiche A Rossi Fanelli and Istituto Pasteur Fondazione Cenci Bolognetti, Universita di Roma Sapienza, Piazzale Aldo Moro 5, 00185 Roma, Italy
Parasitology 134:1215-21. 2007..If calcium channels were correlated with adenosine receptors also in schistosomes, as they are in mammals, this would support the hypothesis that PZQ-induced calcium influx may be correlated to adenosine receptor blockade... - Control of respiration by nitric oxide in Keilin-Hartree particles, mitochondria and SH-SY5Y neuroblastoma cellsD Mastronicola
IFO, Cancer Institute Regina Elena (SSD-SAFU, 00100 Rome, Italy
Cell Mol Life Sci 60:1752-9. 2003..Together the results suggest that the reaction of NO with cytochrome c oxidase in situ follows two alternative inhibition pathways, depending on the electron flux through the respiratory chain... - The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activityE Forte
Department of Biochemical Sciences and CNR Centre of Molecular Biology, University of Rome 'La Sapienza, Rome, Italy
Eur J Biochem 268:6486-91. 2001.... - Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosaK Brown
Architecture et Fonction des Macromolécules Biologiques U M R 6098, C N R S and Universités d Aix Marseille I and II, 31, ch Joseph Aiguier, Marseille Cedex 20, F 13402, France
J Mol Biol 312:541-54. 2001..Moreover they demonstrate that the two histidine residues play a crucial role in the physiological activity of nitrite reduction, ligand binding and in the structural organisation of nitrite reductase from P. aeruginosa... - Binding of NO and CO to the d(1) Heme of cd(1) nitrite reductase from Pseudomonas aeruginosaT K Das
Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA
Biochemistry 40:10774-81. 2001..It is likely that the influence of a highly ruffled structure of heme d(1) on its electronic properties is the major factor causing anomalous Fe-ligand vibrational frequencies... - Fast coordination changes in cytochrome c do not necessarily imply foldingA Arcovito
Istituto Pasteur-Fondazione Cenci Bolognetti e Centro di Biologia Molecolare del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche Alessandro Rossi-Fanelli, , Piazzale Aldo Moro 5, 00185 Roma, Italy
J Biol Chem 276:41073-8. 2001..Rebinding of CO to the four-coordinate heme yields kinetic intermediates unrelated to folding. Our hypothesis is supported by parallel observations carried out with protoheme and microperoxidase... - Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c(551) from Pseudomonas aeruginosaS Gianni
Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Istituto Pasteur-Fondazione Cenci Bolognetti e Centro di Biologia Molecolare del CNR, , Piazzale A. Moro 5, Rome, 00185, Italy
J Mol Biol 309:1177-87. 2001..This strong interaction is stabilized by the hydrogen bond between Trp56 and heme propionate 17 (HP-17) as suggested by the increase in the unfolding rate at high denaturant concentration of the Trp56Phe site-directed mutant... - Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?D Nurizzo
Architecture et Fonction des Macromolecules Biologiques, UPR9039 CNRS, IBSM, 31, ch Joseph Aiguier, Marseille Cedex 20, France
J Biol Chem 274:14997-5004. 1999.... - Primary structure of hemoglobins from trout (Salmo irideus).partial determination of amino acid sequence of HB trout IVF Bossa
FEBS Lett 64:76-80. 1976