Maurizio Brunori

Summary

Affiliation: University of Rome La Sapienza
Country: Italy

Publications

  1. ncbi request reprint Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography
    Paola 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
  2. doi request reprint The Bohr effect before Perutz
    Maurizio 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
  3. doi request reprint Morphogenesis of a protein: folding pathways and the energy landscape
    Maurizio 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
  4. ncbi request reprint Cytochrome c(551) as a model system for protein folding
    Maurizio 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
  5. pmc Myoglobin strikes back
    Maurizio 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
  6. ncbi request reprint Nitric oxide and the respiratory enzyme
    Maurizio 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
  7. pmc Cavities and packing defects in the structural dynamics of myoglobin
    M 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
  8. ncbi request reprint Nitric oxide, cytochrome-c oxidase and myoglobin
    M 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
  9. ncbi request reprint A globin for the brain
    M Brunori
    Istituto Pasteur Fondazione Cenci Bolognetti and Department of Biochemical Sciences, University of Rome La Sapienza, Rome, Italy
    FASEB J 20:2192-7. 2006
  10. ncbi request reprint Control of cytochrome c oxidase activity by nitric oxide
    Maurizio 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

Detail Information

Publications124 found, 100 shown here

  1. ncbi request reprint Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography
    Paola 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...
  2. doi request reprint The Bohr effect before Perutz
    Maurizio 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...
  3. doi request reprint Morphogenesis of a protein: folding pathways and the energy landscape
    Maurizio 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
    ....
  4. ncbi request reprint Cytochrome c(551) as a model system for protein folding
    Maurizio 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...
  5. pmc Myoglobin strikes back
    Maurizio 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...
  6. ncbi request reprint Nitric oxide and the respiratory enzyme
    Maurizio 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...
  7. pmc Cavities and packing defects in the structural dynamics of myoglobin
    M 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...
  8. ncbi request reprint Nitric oxide, cytochrome-c oxidase and myoglobin
    M 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 ..
  9. ncbi request reprint A globin for the brain
    M 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...
  10. ncbi request reprint Control of cytochrome c oxidase activity by nitric oxide
    Maurizio 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...
  11. ncbi request reprint Neuroglobin, seven years after
    M 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...
  12. pmc Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes
    Maurizio 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
    ....
  13. ncbi request reprint Cytochrome c oxidase, ligands and electrons
    Maurizio 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
    ....
  14. ncbi request reprint Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
    Raffaella Musto
    Istituto Pasteur Fondazione Cenci Bolognetti, Universita di Roma La Sapienza, 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...
  15. pmc Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavities
    Cecilia Bossa
    Dipartimento di Chimica, University of Rome La Sapienza, Rome, Italy
    Biophys J 89:465-74. 2005
    ....
  16. ncbi request reprint Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineering
    Stefano 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
    Structure 14:1801-9. 2006
    ..The homologous protein PSD-95 PDZ3 did not display a similar ligand-induced conformational change...
  17. ncbi request reprint Nitrite controls the release of nitric oxide in Pseudomonas aeruginosa cd1 nitrite reductase
    Serena 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...
  18. pmc Molecular dynamics simulation of deoxy and carboxy murine neuroglobin in water
    Massimiliano Anselmi
    Dipartimento di Chimica, Universita di Roma La Sapienza, Rome, Italy
    Biophys J 93:434-41. 2007
    ....
  19. doi request reprint Structural and functional characterization of CcmG from Pseudomonas aeruginosa, a key component of the bacterial cytochrome c maturation apparatus
    Adele 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...
  20. ncbi request reprint Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants
    Elena 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...
  21. ncbi request reprint An on-pathway intermediate in the folding of a PDZ domain
    Ylva 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...
  22. pmc Inhibition of Schistosoma mansoni thioredoxin-glutathione reductase by auranofin: structural and kinetic aspects
    Francesco 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...
  23. doi request reprint NO sensing in Pseudomonas aeruginosa: structure of the transcriptional regulator DNR
    Giorgio 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...
  24. doi request reprint Pattern of cavities in globins: the case of human hemoglobin
    Carmelinda 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...
  25. pmc Mapping the catalytic cycle of Schistosoma mansoni thioredoxin glutathione reductase by X-ray crystallography
    Francesco 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...
  26. ncbi request reprint Redox-linked protonation of cytochrome c oxidase: the effect of chloride bound to CuB
    Elena 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...
  27. ncbi request reprint Controlling ligand binding in myoglobin by mutagenesis
    Federica 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
    ....
  28. ncbi request reprint Fast dissociation of nitric oxide from ferrous Pseudomonas aeruginosa cd1 nitrite reductase. A novel outlook on the catalytic mechanism
    Serena 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...
  29. doi request reprint Glutathione reductase and thioredoxin reductase at the crossroad: the structure of Schistosoma mansoni thioredoxin glutathione reductase
    Francesco 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...
  30. doi request reprint Combining crystallography and molecular dynamics: the case of Schistosoma mansoni phospholipid glutathione peroxidase
    Daniela 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
    ....
  31. pmc The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication
    Fabiana 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...
  32. pmc The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity
    Beatrice 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...
  33. pmc Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain
    Flavio 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...
  34. doi request reprint Observation of fast release of NO from ferrous d₁ haem allows formulation of a unified reaction mechanism for cytochrome cd₁ nitrite reductases
    Serena 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...
  35. ncbi request reprint Kinetic folding mechanism of PDZ2 from PTP-BL
    Stefano 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
    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...
  36. ncbi request reprint Unveiling a hidden folding intermediate in c-type cytochromes by protein engineering
    Alessandro 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...
  37. ncbi request reprint The three-dimensional structure of two redox states of cyclophilin A from Schistosoma mansoni. Evidence for redox regulation of peptidyl-prolyl cis-trans isomerase activity
    Louise 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
    ....
  38. ncbi request reprint The structure of murine neuroglobin: Novel pathways for ligand migration and binding
    Beatrice 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...
  39. pmc The structure of neuroglobin at high Xe and Kr pressure reveals partial conservation of globin internal cavities
    Tommaso 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...
  40. ncbi request reprint Exploring the cytochrome c folding mechanism: cytochrome c552 from thermus thermophilus folds through an on-pathway intermediate
    Carlo 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, Universita di Roma La Sapienza, 00185 Rome, Italy
    J Biol Chem 278:41136-40. 2003
    ....
  41. pmc On the mechanism and rate of gold incorporation into thiol-dependent flavoreductases
    Fulvio Saccoccia
    Department of Biochemical Sciences A Rossi Fanelli, Sapienza University of Rome, Rome, Italy
    J Inorg Biochem 108:105-11. 2012
    ....
  42. ncbi request reprint A common folding mechanism in the cytochrome c family
    Carlo Travaglini-Allocatelli
    Istituto Pasteur Fondazione Cenci Bolognetti, e Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, 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...
  43. ncbi request reprint Critical role of His369 in the reactivity of Pseudomonas aeruginosa cytochrome cd1 nitrite reductase with oxygen
    Fabio Centola
    Department of Biochemical Sciences A Rossi Fanelli, University of Rome La Sapienza, Italy
    FEBS J 273:4495-503. 2006
    ....
  44. doi request reprint New insights into the activity of Pseudomonas aeruginosa cd1 nitrite reductase
    Serena 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...
  45. doi request reprint Fast folding kinetics and stabilization of apo-cytochrome c
    Alessandro 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...
  46. ncbi request reprint Nitric oxide reacts with the single-electron reduced active site of cytochrome c oxidase
    Alessandro 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...
  47. ncbi request reprint Nitric oxide and mitochondrial complex IV
    Paolo 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...
  48. ncbi request reprint Macromolecular bases of antischistosomal therapy
    Francesco Angelucci
    Department of Biochemical Sciences A Rossi Fanelli, Sapienza University of Rome, Italy
    Curr Top Med Chem 11:2012-28. 2011
    ..Moreover, a few enzymes of the parasite are known, or thought, to be "druggable", and therefore interesting, even though no specific drugs are available as yet: examples of such enzymes are Glutathione Peroxidase and Peroxiredoxins...
  49. pmc GB1 is not a two-state folder: identification and characterization of an on-pathway intermediate
    Angela 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...
  50. ncbi request reprint Parallel pathways in cytochrome c(551) folding
    Stefano Gianni
    Istituto Pasteur Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche e Istituto di Biologia e Patologia Molecolari del CNR, Universita di Roma La Sapienza, 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...
  51. ncbi request reprint The O2-scavenging flavodiiron protein in the human parasite Giardia intestinalis
    Adele 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...
  52. ncbi request reprint NO production by Pseudomonas aeruginosa cd1 nitrite reductase
    Francesca 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...
  53. ncbi request reprint Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRF
    Don C Lamb
    Dipartimento di Scienze Biochimiche A Rossi Fanelli, Universita di Roma La Sapienza, 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...
  54. ncbi request reprint Pseudomonas aeruginosa cytochrome C(551): probing the role of the hydrophobic patch in electron transfer
    Francesca 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...
  55. pmc 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...
  56. doi request reprint The folding pathway of a functionally competent C-terminal domain of nucleophosmin: protein stability and denatured state residual structure
    Sara Chiarella
    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 Biophys Res Commun 435:64-8. 2013
    ..The implications of our results are discussed in the context of previous works on single domain helical proteins...
  57. ncbi request reprint The allosteric properties of hemoglobin: insights from natural and site directed mutants
    Andrea 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...
  58. doi request reprint Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways
    Ylva 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...
  59. pmc Structural and functional characterization of Schistosoma mansoni Thioredoxin
    Giovanna 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...
  60. doi request reprint Failure of apoptosis-inducing factor to act as neuroglobin reductase
    Tommaso 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...
  61. pmc A PDZ domain recapitulates a unifying mechanism for protein folding
    Stefano 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...
  62. doi request reprint Neuroglobin: enzymatic reduction and oxygen affinity
    Alessandro 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...
  63. doi request reprint The folding pathway of an engineered circularly permuted PDZ domain
    Ylva 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...
  64. ncbi request reprint Insights into the catalytic mechanism of glutathione S-transferase: the lesson from Schistosoma haematobium
    Francesco 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...
  65. ncbi request reprint Nitric oxide and cytochrome oxidase: reaction mechanisms from the enzyme to the cell
    Paolo 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...
  66. ncbi request reprint An obligatory intermediate in the folding pathway of cytochrome c552 from Hydrogenobacter thermophilus
    Carlo 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...
  67. ncbi request reprint Schistosoma mansoni fatty acid binding protein: specificity and functional control as revealed by crystallographic structure
    Francesco 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...
  68. ncbi request reprint Cytochrome bd, a key oxidase in bacterial survival and tolerance to nitrosative stress
    Elena 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...
  69. ncbi request reprint Plasticity of the protein folding landscape: switching between on- and off-pathway intermediates
    Stefano 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...
  70. pmc Molecular dynamics simulation of the neuroglobin crystal: comparison with the simulation in solution
    Massimiliano 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...
  71. doi request reprint Nitrite reduction: a ubiquitous function from a pre-aerobic past
    Francesca 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...
  72. ncbi request reprint The structural dynamics of myoglobin
    M 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...
  73. ncbi request reprint Cyanide binding to cd(1) nitrite reductase from Pseudomonas aeruginosa: role of the active-site His369 in ligand stabilization
    Wenliang 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...
  74. ncbi request reprint Control of heme reactivity by diffusion: structural basis and functional characterization in hemoglobin mutants
    A 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
    ....
  75. ncbi request reprint Nitric oxide and cellular respiration
    M 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...
  76. ncbi request reprint Photochemically induced electron transfer
    A 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
    ....
  77. ncbi request reprint Identification and characterization of protein folding intermediates
    Stefano 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...
  78. ncbi request reprint Maurizio Brunori turns 70: nothing but a brilliant future behind him
    Gino Amiconi
    Department of Biochemical Sciences, University of Roma La Sapienza, Roma, Italy
    IUBMB Life 59:475-6. 2007
  79. doi request reprint Folding mechanism of the C-terminal domain of nucleophosmin: residual structure in the denatured state and its pathophysiological significance
    Flavio 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
    ....
  80. ncbi request reprint 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
    ....
  81. doi request reprint Structural dynamics of myoglobin
    M 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...
  82. ncbi request reprint Electron entry in a CuA mutant of cytochrome c oxidase from Paracoccus denitrificans. Conclusive evidence on the initial electron entry metal center
    F 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...
  83. pmc The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties
    F 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...
  84. ncbi request reprint Structural dynamics of myoglobin
    M 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...
  85. ncbi request reprint Nitric oxide and cytochrome c oxidase: mechanisms of inhibition and NO degradation
    P 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...
  86. pmc The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin
    M 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
    ....
  87. ncbi request reprint Modulation of mitochondrial respiration by nitric oxide: investigation by single cell fluorescence microscopy
    P 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
    ....
  88. ncbi request reprint The caa3 terminal oxidase of Bacillus stearothermophilus. Transient spectroscopy of electron transfer and ligand binding
    A 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...
  89. ncbi request reprint Sulfolobus acidocaldarius terminal oxidase. A kinetic investigation and its structural interpretation
    A 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...
  90. ncbi request reprint The oxygen reactive species of cytochrome-c-oxidase: an alternative view
    M Brunori
    Department of Biochemical Sciences, University of Rome, La Sapienza, Italy
    FEBS Lett 314:191-4. 1992
    ....
  91. ncbi request reprint N-oxide sensing and denitrification: the DNR transcription factors
    S 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
    ....
  92. ncbi request reprint 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...
  93. ncbi request reprint [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)...
  94. ncbi request reprint [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...
  95. ncbi request reprint Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant
    Adriana 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...
  96. doi request reprint Distinguishing between smooth and rough free energy barriers in protein folding
    Stefano 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...
  97. doi request reprint 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
  98. ncbi request reprint Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium
    Kenneth 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...
  99. ncbi request reprint Control of electron transfer by the electrochemical potential gradient in cytochrome-c oxidase reconstituted into phospholipid vesicles
    P 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...
  100. ncbi request reprint Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c(551) from Pseudomonas aeruginosa
    S 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...
  101. ncbi request reprint Spectral analysis of cytochromes in rat heart myocytes: transient and steady-state photodiode array spectrophotometry measurements
    P 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)...