Research Topics
Genomes and Genes | Maurizio BrunoriSummaryAffiliation: University of Rome La Sapienza Country: Italy Publications
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Publications
Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallographyPaola Baiocco
Department of Biochemical Sciences A. Rossi Fanelli and Istituto Pasteur- Fondazione Cenci Bolognetti, University of Rome La Sapienza, Rome, Italy
J Mol Biol 360:678-89. 2006..These rearrangements are coupled to quaternary rigid-body movements at the dimer interface and alterations in the localisation and structural order of the C-terminal domain...
The Bohr effect before PerutzMaurizio Brunori
Department of Biochemical Sciences, Sapienza University of Rome, p le A Moro, 5 00185 Roma, Italy
Biochem Mol Biol Educ 40:297-9. 2012..F. Perutz, paved the way to the concept of allostery. After 1960 the availability of the crystallographic structure opened new horizons to the interpretation of the allosteric properties of hemoglobin...- Morphogenesis of a protein: folding pathways and the energy landscapeMaurizio Brunori
Istituto Pasteur Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Rome, Italy
Biochem Soc Trans 40:429-32. 2012.... - 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... - Control of cytochrome c oxidase activity by nitric oxideMaurizio Brunori
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, Piazzale Aldo Moro 5, I 00185 Rome, Italy
Biochim Biophys Acta 1655:365-71. 2004..The aim of this work is to review the information available on these two mechanisms of inhibition of respiration... 
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...- 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... - Myoglobin strikes backMaurizio Brunori
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Sapienza Universita di Roma, Piazzale A Moro 5, 00185 Roma, Italy
Protein Sci 19:195-201. 2010..This approach unveiled the complexity of the energy landscape and the structural basis of the stretched interconversion between conformational substates of a protein... - Nitric oxide and the respiratory enzymeMaurizio Brunori
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, I 00185 Rome, Italy
Biochim Biophys Acta 1757:1144-54. 2006..We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase... - Cytochrome c(551) as a model system for protein foldingMaurizio Brunori
Istituto Pasteur Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Universita di Roma La Sapienza, P le A Moro 5, 00185 Roma, Italy
Biophys Chem 100:409-19. 2003..Comparison of our results with those obtained by others on horse heart cytochrome c allows to draw some general conclusions on the structural features that are common determinants in the folding of members of the cytochrome c family... - Cytochrome c oxidase, ligands and electronsMaurizio Brunori
Department of Biochemical Sciences A Rossi Fanelli and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, P le Aldo Moro, 5, I 00185 Roma, Italia
J Inorg Biochem 99:324-36. 2005.... - Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changesMaurizio Brunori
Department of Biochemical Sciences and Consiglio Nazionale delle Ricerche Institute of Molecular Biology and Pathology, University of Rome La Sapienza, 00185 Rome, Italy
Proc Natl Acad Sci U S A 102:8483-8. 2005.... - 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 .. - Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globinsRaffaella Musto
Istituto Pasteur-Fondazione Cenci Bolognetti, , Piazzale A. Moro 5, 00185 Rome, Italy
Biochemistry 43:230-6. 2004..This residue thus plays a role which is evolutionarily conserved in the globin family from invertebrates to mammals; our results support the contention that the A-G-H cluster is important in the folding pathway of different globins... - Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavitiesCecilia Bossa
Dipartimento di Chimica, University of Rome La Sapienza, Rome, Italy
Biophys J 89:465-74. 2005.... - Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineeringStefano Gianni
Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, , Piazzale A. Moro 5, 00185 Rome, Italy
Structure 14:1801-9. 2006..The homologous protein PSD-95 PDZ3 did not display a similar ligand-induced conformational change... - Molecular dynamics simulation of deoxy and carboxy murine neuroglobin in waterMassimiliano Anselmi
Dipartimento di Chimica, Universita di Roma La Sapienza, Rome, Italy
Biophys J 93:434-41. 2007.... - Structural and functional characterization of CcmG from Pseudomonas aeruginosa, a key component of the bacterial cytochrome c maturation apparatusAdele Di Matteo
Dipartimento di Scienze Biochimiche, Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Universita di Roma, Piazzale A Moro 5, 00185, Roma, Italy
Proteins 78:2213-21. 2010..This observation suggests that, in vivo, the physiological substrate of Pa-CcmG may be the mixed-disulfide complex between Pa-CcmH and apo-cyt... - An on-pathway intermediate in the folding of a PDZ domainYlva Ivarsson
Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Piazzale A Moro 5, 00185 Rome, Italy
J Biol Chem 282:8568-72. 2007..The results presented exemplify a novel type of kinetic test to detect an on-pathway folding intermediate... - Nitrite controls the release of nitric oxide in Pseudomonas aeruginosa cd1 nitrite reductaseSerena Rinaldo
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Sapienza Universita di Roma, p le A Moro, 5 00185 Rome, Italy
Biochem Biophys Res Commun 363:662-6. 2007..Thus we suggest that also in vivo the activity of cd1NIR is controlled by nitrite... - NO sensing in Pseudomonas aeruginosa: structure of the transcriptional regulator DNRGiorgio Giardina
Department of Biochemical Sciences A Rossi Fanelli, University of Rome La Sapienza, 00185 Rome, Italy
J Mol Biol 378:1002-15. 2008..Preliminary experiments indicate that heterologous expression of the heme-containing DNR yields a protein able to bind DNA in vitro... - Inhibition of Schistosoma mansoni thioredoxin-glutathione reductase by auranofin: structural and kinetic aspectsFrancesco Angelucci
Department of Biochemical Sciences A Rossi Fanelli, Sapienza University of Rome and Istituto Pasteur Fondazione Cenci Bolognetti, P le Aldo Moro 5, 00185 Rome, Italy
J Biol Chem 284:28977-85. 2009..Therefore, we propose that Sec mediates the transfer of gold from its ligands in AF to the redox-active Cys couples of TGR... - Mapping the catalytic cycle of Schistosoma mansoni thioredoxin glutathione reductase by X-ray crystallographyFrancesco Angelucci
Department of Biochemical Sciences A Rossi Fanelli, CNR Institute of Molecular Biology and Pathology and Istituto Pasteur Fondazione Cenci Bolognetti, Sapienza University of Rome, P le Aldo Moro 5, 00185 Rome, Italy
J Biol Chem 285:32557-67. 2010..mansoni TGR. In particular, we hereby propose the putative functionally relevant conformational change of the C terminus after the transfer of reducing equivalents from NADPH to the redox sites of the enzyme... - Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutantsElena Forte
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, I-00185 Rome, Italy
Biochemistry 43:2957-63. 2004..5 H(+) transferred (at least partially) through the K-pathway. On the basis of these results, the possible involvement of the D-pathway in the redox-linked protonation of cytochrome c oxidase is discussed... - Pattern of cavities in globins: the case of human hemoglobinCarmelinda Savino
University of Rome, P le Aldo Moro 5, 00185 Rome, Italy
Biopolymers 91:1097-107. 2009..The number and position of hydrophobic cavities in hemoglobin are briefly discussed also in comparison with the data available for other members of the globin superfamily... - Controlling ligand binding in myoglobin by mutagenesisFederica Draghi
A. Rossi Fanelli Department of Biochemical Sciences, CNR Center of Molecular Biology, University of Rome La Sapienza, P. le. A. Moro 5, 00185 Rome, Italy
J Biol Chem 277:7509-19. 2002.... - Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domainFlavio Scaloni
Istituto Pasteur Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Rome, Italy
Proc Natl Acad Sci U S A 107:5447-52. 2010..Our observations constitute the essential prerequisite for structure-based drug-design studies, aimed at identifying molecules that may rescue pathological NPM1 mutants by stabilizing the native-like state... - The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replicationFabiana Renzi
Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, 00185 Rome, Italy
Proc Natl Acad Sci U S A 103:12365-70. 2006..The conserved structural determinants of this site may provide a framework for attempting to design antiviral drugs to interfere with the infectious nidovirus life cycle... - The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinityBeatrice Vallone
Department of Biochemical Sciences and Istituto Pasteur Fondazione Cenci Bolognetti, University of Rome La Sapienza, Piazzale A Moro 5, 00185 Rome, Italy
Proc Natl Acad Sci U S A 101:17351-6. 2004..This unexpected structural change unveils a heme-sliding mechanism of affinity control that may be of significance to understanding Ngb's role in the pathophysiology of the brain... - Combining crystallography and molecular dynamics: the case of Schistosoma mansoni phospholipid glutathione peroxidaseDaniela Dimastrogiovanni
Dipartimento di Scienze Biochimiche A Rossi Fanelli and Istituto Pasteur, Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome, Italy
Proteins 78:259-70. 2010.... - Fast dissociation of nitric oxide from ferrous Pseudomonas aeruginosa cd1 nitrite reductase. A novel outlook on the catalytic mechanismSerena Rinaldo
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, 00185 Rome, Italy
J Biol Chem 282:14761-7. 2007..This finding also provides a rationale for the presence in cd(1) NIR of the peculiar d(1)-heme cofactor, which has probably evolved to ensure fast product dissociation... - Glutathione reductase and thioredoxin reductase at the crossroad: the structure of Schistosoma mansoni thioredoxin glutathione reductaseFrancesco Angelucci
Department of Biochemical Sciences A Rossi Fanelli, Istituto Pasteur Fondazione Cenci Bolognetti and CNR Institute of Molecular Biology and Pathology, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy
Proteins 72:936-45. 2008..These data update the interpretation of the interdomain communication in TGR enzymes. The possible function of this enzyme in pathogenic parasites is discussed... - Observation of fast release of NO from ferrous d₁ haem allows formulation of a unified reaction mechanism for cytochrome cd₁ nitrite reductasesSerena Rinaldo
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Sapienza Universita di Roma, P A Moro, 5 00185 Rome, Italy
Biochem J 435:217-25. 2011..We present a reaction mechanism proposed to be applicable to all cytochromes cd1 and conclude that the d1 haem has evolved to have low affinity for NO, as compared with other ferrous haems... - Kinetic folding mechanism of PDZ2 from PTP-BLStefano Gianni
Istituto Pasteur-Fondazione Cenci Bolognetti e Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, , Piazzale A. Moro 5, 00185 Rome, Italy
Protein Eng Des Sel 18:389-95. 2005..1 to 8.0 or in the presence of a stabilizing salt) and also data on a site-directed conservative mutant can be rationalized in terms of a simple reaction scheme involving a single set of intermediates and transition states... - The structure of murine neuroglobin: Novel pathways for ligand migration and bindingBeatrice Vallone
Department of Biochemical Sciences, University of Rome La Sapienza, Rome, Italy
Proteins 56:85-92. 2004..Based on this high-resolution structure, further structure-function studies can be planned to elucidate the role of neuroglobin in physiological responses to hypoxia... - Redox-linked protonation of cytochrome c oxidase: the effect of chloride bound to CuBElena Forte
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, I-00185 Rome, Italy
Biochemistry 41:13046-52. 2002..The relevance of this finding to the understanding of the enzyme mechanism is discussed... - Unveiling a hidden folding intermediate in c-type cytochromes by protein engineeringAlessandro Borgia
Istituto Pasteur Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, P le A Moro 5, 00185 Rome, Italy
J Biol Chem 281:9331-6. 2006..These results show how protein engineering, x-ray crystallography and state-of-the-art kinetics concur to unveil a folding intermediate and the structural determinants of its stability... - The structure of neuroglobin at high Xe and Kr pressure reveals partial conservation of globin internal cavitiesTommaso Moschetti
Department of Biochemical Sciences A Rossi Fanelli, University of Rome La Sapienza, Rome, Italy
Biophys J 97:1700-8. 2009..This may be of significance in connection with the redox chemistry that may be the primary function of this hexacoordinate globin... - The three-dimensional structure of two redox states of cyclophilin A from Schistosoma mansoni. Evidence for redox regulation of peptidyl-prolyl cis-trans isomerase activityLouise J Gourlay
Istituto Pasteur Fondazione Cenci Bolognetti, Department of Biochemical Sciences A Rossi Fanelli, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy
J Biol Chem 282:24851-7. 2007.... - Exploring the cytochrome c folding mechanism: cytochrome c552 from thermus thermophilus folds through an on-pathway intermediateCarlo Travaglini-Allocatelli
Istituto Pasteur-Fondazione Cenci Bolognetti e Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, , 00185 Rome, Italy
J Biol Chem 278:41136-40. 2003.... - On the mechanism and rate of gold incorporation into thiol-dependent flavoreductasesFulvio Saccoccia
Department of Biochemical Sciences A Rossi Fanelli, Sapienza University of Rome, Rome, Italy
J Inorg Biochem 108:105-11. 2012.... - A common folding mechanism in the cytochrome c familyCarlo Travaglini-Allocatelli
Istituto Pasteur-Fondazione Cenci Bolognetti, e Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche, , Rome, Italy
Trends Biochem Sci 29:535-41. 2004..This novel outlook on the folding of cyt c can shed light on much published data and might offer a general scheme by which to plan new experiments... - Nitric oxide and mitochondrial complex IVPaolo Sarti
Department of Biochemical Sciences, University of Rome La Sapienza 1 00185 Rome, Italy
IUBMB Life 55:605-11. 2003..Among a number of parameters that appear to control the switch over between the two mechanisms, the concentration of reductants (reduced cytochrome c) at the cytochrome c oxidase site has been proved to be the most relevant one... - Critical role of His369 in the reactivity of Pseudomonas aeruginosa cytochrome cd1 nitrite reductase with oxygenFabio Centola
Department of Biochemical Sciences A. Rossi Fanelli, University of Rome La Sapienza, Italy
FEBS J 273:4495-503. 2006.... - Nitric oxide reacts with the single-electron reduced active site of cytochrome c oxidaseAlessandro Giuffrè
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, I 00185 Rome, Italy
J Biol Chem 277:22402-6. 2002..denitrificans and from beef heart. Results also suggest that the H(+)-conducting K pathway, but not the D pathway, controls the kinetics of the single-electron reduction of the active site... - Fast folding kinetics and stabilization of apo-cytochrome cAlessandro Borgia
Dipartimento di Scienze Biochimiche, A Rossi Fanelli, Sapienza, Universita di Roma, Piazzale A Moro 5, 00185 Rome, Italy
FEBS Lett 582:1003-7. 2008..These results challenge current thinking about the role of the heme group in the folding of c-type cytochromes... - New insights into the activity of Pseudomonas aeruginosa cd1 nitrite reductaseSerena Rinaldo
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Istituto di Biologia e Patologia Molecolari del CNR, Sapienza, Universita di Roma, Rome, Italy
Biochem Soc Trans 36:1155-9. 2008..These results shed light on the mechanistic details of the activity of cd(1) nitrite reductases and on the biological role of the d(1)-haem, whose presence in this class of enzymes has to date been unexplained... - Macromolecular bases of antischistosomal therapyFrancesco Angelucci
Department of Biochemical Sciences A Rossi Fanelli, Sapienza University of Rome, Italy
Curr Top Med Chem 11:2012-28. 2011.... - GB1 is not a two-state folder: identification and characterization of an on-pathway intermediateAngela Morrone
Istituto Pasteur Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Rome, Italy
Biophys J 101:2053-60. 2011..Failure to identify the presence of an intermediate affects some of the conclusions that have been drawn for GB1, a popular model for protein folding studies... - The O2-scavenging flavodiiron protein in the human parasite Giardia intestinalisAdele Di Matteo
Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology and Istituto Pasteur Fondazione Cenci Bolognetti, Sapienza, University of Rome, Rome I 00185, Italy
J Biol Chem 283:4061-8. 2008..We propose that in G. intestinalis the primary function of FDP is to efficiently scavenge O(2), allowing this microaerobic parasite to survive in the human small intestine, thus promoting its pathogenicity... - Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRFDon C Lamb
Dipartimento di Scienze Biochimiche A. Rossi Fanelli, , Piazzale Aldo Moro 5, 00185 Rome, Italy
Biophys Chem 109:41-58. 2004..Above approximately 180 K, ligands migrate to the proximal Xe1 site (D) and also exit into the solvent, from where they rebind in a bimolecular reaction... - Parallel pathways in cytochrome c(551) foldingStefano Gianni
Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche e Istituto di Biologia e Patologia Molecolari del CNR, , Piazzale A. Moro 5, 00185 Rome, Italy
J Mol Biol 330:1145-52. 2003..These findings indicate the presence of two or more slowly inter-converting ensembles of denatured states that give rise to pH-dependent partitioning among fast and slow-folding pathways... - Pseudomonas aeruginosa cytochrome C(551): probing the role of the hydrophobic patch in electron transferFrancesca Cutruzzola
Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, P le A Moro 5, 00185 Rome, Italy
J Inorg Biochem 88:353-61. 2002..aeruginosa azurin, a copper protein often used as a model redox partner in vitro. Our results show that introduction of a negative charge in the hydrophobic patch severely hampers both homonuclear and heteronuclear electron transfer... - NO production by Pseudomonas aeruginosa cd1 nitrite reductaseFrancesca Cutruzzola
Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, 00185 Rome, Italy
IUBMB Life 55:617-21. 2003..The positive potential in the active site is largely due to the presence of the two conserved distal histidines, which are involved in both substrate binding and product release... - Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10)M Brunori
Department of Biochemical Sciences and CNR Center of Molecular Biology, University of Rome La Sapienza, Rome, Italy
Biophys J 76:1259-69. 1999..This interpretation suggests that very fast (picosecond) fluctuations of amino acid side chains may play a crucial role in controlling O2 delivery to tissue at a rate compatible with physiology... - The allosteric properties of hemoglobin: insights from natural and site directed mutantsAndrea Bellelli
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita degli Studi di Roma La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy
Curr Protein Pept Sci 7:17-45. 2006..Occasional reference is made to site directed mutants of myoglobin, whenever this helps clarifying perplexing results obtained on hemoglobin... - The folding pathway of an engineered circularly permuted PDZ domainYlva Ivarsson
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Sapienza Universita di Roma, Piazzale A, Rome, Italy
Protein Eng Des Sel 21:155-60. 2008..The results support the importance of sequence connectivity both in the mechanism and the speed of protein folding... - Insights into the catalytic mechanism of glutathione S-transferase: the lesson from Schistosoma haematobiumFrancesco Angelucci
Istituto di Biologia e Patologia Molecolari del CNR, Department of Biochemical Sciences A. Rossi Fanelli, University of Rome La Sapienza, 00185 Rome, Italy
Structure 13:1241-6. 2005..Arginine and two other residues of the external pocket constitute a conserved structural motif, clearly identified by sequence comparison... - Neuroglobin: enzymatic reduction and oxygen affinityAlessandro Giuffrè
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, Sapienza University of Rome, I 00185 Rome, Italy
Biochem Biophys Res Commun 367:893-8. 2008..Interestingly, E. coli FlRd-red shares sequence similarity with the FAD-binding domain of the human apoptosis-inducing factor, a finding which may have unexpected significance with reference to the mechanism of neuroprotection by Ngb... - A PDZ domain recapitulates a unifying mechanism for protein foldingStefano Gianni
Istituto Pasteur Fondazione Cenci Bolognetti e Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Piazzale A Moro 5, 00185 Rome, Italy
Proc Natl Acad Sci U S A 104:128-33. 2007..The analysis of the (un)folding kinetics for other three-state proteins (when available) appears consistent with the predictions ensuing from this unifying mechanism, thus providing a powerful validation of its general nature... - Nitric oxide and cytochrome oxidase: reaction mechanisms from the enzyme to the cellPaolo Sarti
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, Rome, Italy
Free Radic Biol Med 34:509-20. 2003..In particular, the role played by CcOX in protecting the cell from excess NO, potentially toxic for mitochondria, is also reviewed highlighting the mechanistic differences between eukaryotes and some prokaryotes... - An obligatory intermediate in the folding pathway of cytochrome c552 from Hydrogenobacter thermophilusCarlo Travaglini-Allocatelli
Istituto Pasteur Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, P le A Moro 5, 00185, Roma Italy
J Biol Chem 280:25729-34. 2005..Analysis of the folding kinetics and correlation with the three-dimensional structure add new evidence for the validity of a consensus folding mechanism in the cytochrome c family... - Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathwaysYlva Ivarsson
Istituto Pasteur Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Piazzale A Moro 5, 00185 Rome, Italy
J Am Chem Soc 131:11727-33. 2009..The results suggest that folding is driven by competing nuclei whose stabilities may be selectively tuned by circular permutation... - Failure of apoptosis-inducing factor to act as neuroglobin reductaseTommaso Moschetti
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, Sapienza University of Rome, I 00185 Rome, Italy
Biochem Biophys Res Commun 390:121-4. 2009..In this study, we tested this hypothesis and show that the Ngb-reductase activity of recombinant human AIF is negligible and hence incompatible with such a physiological function... - Structural and functional characterization of Schistosoma mansoni ThioredoxinGiovanna Boumis
Dipartimento di Scienze Biochimiche and Istituto Pasteur Fondazione Cenci Bolognetti, Sapienza University of Rome, P le Aldo Moro 5, 00185 Rome, Italy
Protein Sci 20:1069-76. 2011..We believe its crystal structure may provide clues for the formation of granulomas and the pathogenesis of the chronic disease... - Schistosoma mansoni fatty acid binding protein: specificity and functional control as revealed by crystallographic structureFrancesco Angelucci
Department of Biochemical Sciences A. Rossi Fanelli, CNR Institute of Molecular Biology and Pathology and Istituto Pasteur-Fondazione Cenci Bolognetti, University of Rome La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy
Biochemistry 43:13000-11. 2004..The binding rate constant of ligands is controlled by a slow pH dependent conformational change, which we propose to have physiological relevance... - Molecular dynamics simulation of the neuroglobin crystal: comparison with the simulation in solutionMassimiliano Anselmi
Dipartimento di Chimica and Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, Rome, Italy
Biophys J 95:4157-62. 2008..The results show that the different environments (crystal or solution) affect the dynamics of the heme group and of the CD corner... - Plasticity of the protein folding landscape: switching between on- and off-pathway intermediatesStefano Gianni
Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Universita di Roma, P le A Moro 5, 00185, Roma, Italy
Arch Biochem Biophys 466:172-6. 2007..We present evidence that, by destabilizing the relevant transition state, the native state of HT cyt c(552) can be reached along alternative folding routes, which may involve an off-pathway intermediate... - Cytochrome bd, a key oxidase in bacterial survival and tolerance to nitrosative stressElena Forte
Department of Biochemical Sciences, Sapienza University of Rome, Rome, Italy
Ital J Biochem 56:265-9. 2007..In this minireview we discuss the properties of the reactions between bd-type oxidases and NO, and highlight consequences to cell/bacteria physiology... - Nitrite reduction: a ubiquitous function from a pre-aerobic pastFrancesca Cutruzzola
Dipartimento di Scienze Biochimiche A Rossi Fanelli, Sapienza Universita di Roma, Rome, Italy
Bioessays 31:885-91. 2009..The evidence that nitrite reductase activities of enzymes with different cellular roles and biochemical features still exist today highlights the importance of nitrite in cellular homeostasis... - 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... - Cyanide binding to cd(1) nitrite reductase from Pseudomonas aeruginosa: role of the active-site His369 in ligand stabilizationWenliang Sun
Dipartimento di Scienze Biochimiche A Rossi Fanelli and Centro di Biologia Molecolare del CNR, Universita di Roma La Sapienza, Rome, Italy
Biochem Biophys Res Commun 291:1-7. 2002..These results suggest that in Pa cd(1) NiR the invariant distal residue His369 plays a dominant role in controlling the binding of anionic ligands and allow the discussion of the mechanism of cyanide binding to the wild-type enzyme... - 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.... - 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.... - 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... - Folding mechanism of the C-terminal domain of nucleophosmin: residual structure in the denatured state and its pathophysiological significanceFlavio Scaloni
Istituto Pasteur Fondazione Cenci Bolognetti and Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Rome, Italy
FASEB J 23:2360-5. 2009.... - Identification and characterization of protein folding intermediatesStefano Gianni
Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Piazzale A Moro 5, 00185 Rome, Italy
Biophys Chem 128:105-13. 2007..Here we summarize some of the experimental approaches aimed at the detection and characterization of folding intermediates along with a discussion of some general structural features emerging from these studies... - Maurizio Brunori turns 70: nothing but a brilliant future behind himGino Amiconi
Department of Biochemical Sciences, University of Roma La Sapienza, Roma, Italy
IUBMB Life 59:475-6. 2007 - Roles for holes: are cavities in proteins mere packing defects?Beatrice Vallone
Dipartimento di Scienze Biochimiche, A Rossi Fanelli, Universita di Roma La Sapienza Roma Italy
Ital J Biochem 53:46-52. 2004.... - Electron entry in a CuA mutant of cytochrome c oxidase from Paracoccus denitrificans. Conclusive evidence on the initial electron entry metal centerF Malatesta
Department of Biochemical Sciences A Rossi Fanelli and CNR Centre of Molecular Biology, University of Rome La Sapienza, Italy
FEBS Lett 434:322-4. 1998..100 mV lower than the wild type, and that internal electron transfer to cytochrome a is > or = 10(3)-fold slower than with the wild type 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... - 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... - 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... - 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... - 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.... - 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... - 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.... - 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.... - [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... - Modulation of mitochondrial respiration by nitric oxide: investigation by single cell fluorescence microscopyP Sarti
Department of Biochemical Sciences A Rossi Fanelli and CNR Center of Molecular Biology, University of Rome La Sapienza, I 00185 Roma
FASEB J 13:191-7. 1999.... - 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... - 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... - [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)... - Distinguishing between smooth and rough free energy barriers in protein foldingStefano Gianni
Istituto Pasteur Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, Rome, Italy
Biochemistry 48:11825-30. 2009..We show that such an analysis represents a valuable test for the discrimination between the two different scenarios... - Is neuroglobin a signal transducer?Alessandro Giuffrè
Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology, Sapienza University of Rome, Piazzale Aldo Moro 5, I 00185 Rome, Italy
IUBMB Life 60:410-3. 2008 - Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutantAdriana E Miele
Dipartimento di Scienze Biochimiche and CNR Istituto di Biologia e Patologia Molecolari, Universita di Roma La Sapienza, P.le A. Moro 5, 00185 Rome, Italy
Acta Crystallogr D Biol Crystallogr 59:982-8. 2003..Improvement of the stereochemical parameters of a protein structure is fundamental to quantitative analysis of its function and dynamics and hence to thorough understanding of the molecular mechanisms of action... - Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobiumKenneth A Johnson
Department of Biochemical Sciences and Istituto Pasteur-Fondazione Cenci Bolognetti, University of Rome La Sapienza, Rome, Italy
Biochemistry 42:10084-94. 2003..The relatively tight binding of GSH by Sh28GST explains the residually bound GSH in the crystal and supports a possible role of GSH as a tightly bound cofactor involved in the catalytic mechanism for prostaglandin D(2) synthase activity... - 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... - Kinetic control of internal electron transfer in cytochrome c oxidaseM Brunori
Department of Biochemical Sciences A Rossi Fanelli, University of Rome La Sapienza, Italy
Biofactors 8:191-3. 1998..We conclude that in the oxidized enzyme the two hemes are not in very rapid redox equilibrium and internal eT is kinetically controlled... - 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... - 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...