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Genomes and Genes | I BertiniSummaryAffiliation: University of Florence Country: Italy Publications
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Publications
Structural basis for matrix metalloproteinase 1-catalyzed collagenolysisIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 134:2100-10. 2012..The aforementioned steps provide a detailed, experimentally derived, and energetically favorable collagenolytic mechanism, as well as significant insight into the roles of distinct domains in extracellular protease function...
NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(556)Ivano Bertini
CERM and Department of Chemistry, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Inorg Chem 9:224-30. 2004..The directions and magnitude of the magnetic susceptibility anisotropy tensor were also calculated. The approach readily provides useful results, especially for paramagnetic metalloproteins of moderate to large dimensions...- 13C-13C NOESY: an attractive alternative for studying large macromoleculesIvano Bertini
CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Am Chem Soc 126:464-5. 2004.... - Thermotoga maritima IscU. Structural characterization and dynamics of a new class of metallochaperoneIvano Bertini
Magnetic Resonance Center, University of Florence, Via L Sacconi, 6 50019 Sesto Fiorentino, Italy
J Mol Biol 331:907-24. 2003..Additionally, the fluxionality of IscU is unique in that the protein appears to be more compact (based on 1H/2H exchange, R1, R2, and NOE data) but yet more fluid (lack of long-range NOEs) than typical molten globule proteins... - Tuning the affinity for lanthanides of calcium binding proteinsIvano Bertini
Magnetic Resonance Center and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
Biochemistry 42:8011-21. 2003..Finally, by using CaM samples containing only three of the four calcium ions, it was possible to prepare well-defined Ca(3)Ln-CaM derivatives (Ln = Tb, Dy, Tm, and Yb), with interesting properties as NMR probes... - A use of Ramachandran potentials in protein solution structure determinationsIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Biomol NMR 26:355-66. 2003..The quality of the structures, and of Ramachandran plot statistics in particular, was notably improved while preserving the agreement with the experimental constraints... - X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinasesIvano Bertini
Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 42:2673-6. 2003 - The magnetic properties of myoglobin as studied by NMR spectroscopyIvano Bertini
CERM, University of Florence, Via Luigi Sacconi 6 50019 Sesto Fiorentino, Florence, Italy
Chemistry 9:2316-22. 2003.... - The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactomeIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Sesto Fiorentino, Florence, Italy
PLoS ONE 6:e18329. 2011..The present model provides insights to the mechanism by which cytochrome c translocated to cytosol can be intercepted, so that the apoptosome is not assembled... - Bioinorganic chemistry in the postgenomic eraIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 100:3601-4. 2003..The "case study" of metal homeostasis in cells is discussed to provide a flavor of the current evolution of the field... - A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome cIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 42:3457-63. 2003.... - 13C direct detected experiments: optimization for paramagnetic signalsIvano Bertini
Magnetic Resonance Center, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Magn Reson 174:125-32. 2005.... - Application of NMRD to hydration of rubredoxin and a variant containing a (Cys-S)3FeIII(OH) siteIvano Bertini
CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biophys J 84:545-51. 2003..1)H nuclear magnetic relaxation dispersion profiles indicate increased hydration with respect to the wild-type... - Cross correlation rates between Curie spin and dipole-dipole relaxation in paramagnetic proteins: the case of cerium substituted calbindin D9kIvano Bertini
Magnetic Resonance Center, University of Florence, Italy
J Biomol NMR 23:115-25. 2002..This integrated structure calculation protocol has the advantage that different paramagnetic-based constraints are treated by the same algorithm in a way that the efficiency of each class of constraints can be analyzed and compared... - Efficiency of paramagnetism-based constraints to determine the spatial arrangement of alpha-helical secondary structure elementsIvano Bertini
CERM and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
J Biomol NMR 22:123-36. 2002..In cases like calbindin D9k, the availability of datasets from different metal ions is helpful, whereas less important is the location of the metal ion with respect to the secondary structure elements... - Locating the metal ion in calcium-binding proteins by using cerium(III) as a probeI Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
Chembiochem 2:550-8. 2001.... - Cytochrome c and SDS: a molten globule protein with altered axial ligationIvano Bertini
CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Mol Biol 336:489-96. 2004..Such findings are meaningful with respect to the physiology of cytochrome c as electron transfer protein and as promoter of apoptosis... - Crystal structure of the catalytic domain of human matrix metalloproteinase 10I Bertini
CERM, University of Florence and FiorGen Foundation, Via Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Mol Biol 336:707-16. 2004..Furthermore, the binding mode of N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH), which is one of the most known commercial inhibitors of MMPs, is described for the first time... 
Bioinformatics in bioinorganic chemistryIvano Bertini
Magnetic Resonance Center CERM University of Florence, Via L Sacconi 6, Sesto Fiorentino, Italy
Metallomics 2:39-51. 2010..We show how metalloproteomes can be extracted from genome sequences, how structural properties can be related to function, how databases can be implemented, and how hints on interactions can be obtained from bioinformatics...- The annotation of full zinc proteomesIvano Bertini
Magnetic Resonance Center CERM, Department of Chemistry, University of Florence, Via L Sacconi 6, 50019, Sesto Fiorentino, Italy
J Biol Inorg Chem 15:1071-8. 2010..Among the findings, we have propose a zinc binding site for archaeal zinc-importing proteins. Furthermore, we propose two groups of transcriptional regulators that are involved in fatty acid metabolism... - High-resolution solid-state NMR structure of a 17.6 kDa proteinIvano Bertini
Magnetic Resonance Center, CERM, University of Florence, Via L Sacconi, 6 50019 Sesto Fiorentino, Italy
J Am Chem Soc 132:1032-40. 2010..3 A). The proposed strategy, which may be generalized for nonmetalloproteins with the use of paramagnetic tags, represents a significant step ahead in protein structure determination using solid-state NMR... - Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidinI Bertini
Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy
J Med Chem 52:4838-43. 2009..All these structures will provide the basis for the rational design of new cantharidin-based drugs... - Individual human phenotypes in metabolic space and timePatrizia Bernini
Magnetic Resonance Center CERM, University of Florence, Sesto Fiorentino, Italy
J Proteome Res 8:4264-71. 2009.... - The metabonomic signature of celiac diseaseIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Proteome Res 8:170-7. 2009..Altered serum levels of glucose and ketonic bodies suggest alterations of energy metabolism, while the urine data point to alterations of gut microbiota. Metabolomics may thus provide further hints on the biochemistry of the disease... - Water-based ligand screening for paramagnetic metalloproteinsIvano Bertini
Magnetic Resonance Center (CERM, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 47:4533-7. 2008 - Cytochrome c: occurrence and functionsIvano Bertini
Magnetic Resonance Center (CERM, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Chem Rev 106:90-115. 2006 - Combining in silico tools and NMR data to validate protein-ligand structural models: application to matrix metalloproteinasesIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Med Chem 48:7544-59. 2005..This protocol is proposed as a viable alternative to the many approaches described in the literature... - A structural model for the adduct between cytochrome c and cytochrome c oxidaseIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Biol Inorg Chem 10:613-24. 2005.... - (13)C-(13)C NOESY: a constructive use of (13)C-(13)C spin-diffusionIvano Bertini
Magnetic Resonance Center and Department of Chemistry, University of Florence, Italy
J Biomol NMR 30:245-51. 2004..The interpretation was confirmed by simulations. This approach broadens the range of applicability of (13)C-(13)C NOESY spectroscopy... - NMR spectroscopic detection of protein protons and longitudinal relaxation rates between 0.01 and 50 MHzIvano Bertini
Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 44:2223-5. 2005 - Persistent contrast enhancement by sterically stabilized paramagnetic liposomes in murine melanomaIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Italy
Magn Reson Med 52:669-72. 2004..High persistence of the CA was also observed in the liver and intestine, as expected in a hepatobiliar excretion pathway... - Experimentally exploring the conformational space sampled by domain reorientation in calmodulinIvano Bertini
Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 101:6841-6. 2004..The same approach is in principle applicable to other multidomain proteins, as well as to multiple interaction modes between two macromolecular partners... - Paramagnetism-based versus classical constraints: an analysis of the solution structure of Ca Ln calbindin D9kI Bertini
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
J Biomol NMR 21:85-98. 2001.... - Model-free analysis of a thermophilic Fe(7)S(8) protein compared with a mesophilic Fe(4)S(4) proteinI Bertini
Department of Chemistry, University of Florence, Florence, Italy
Proteins 41:75-85. 2000..This research shows that subnanosecond rigidity is not related to thermostability and provides an estimate of the effect of increasing temperature on this time scale... - Lanthanide induced residual dipolar couplings for the conformational investigation of peripheral 15NH2 moietiesI Bertini
Magnetic Resonance Center CERM, University of Florence, Italy
J Biomol NMR 18:347-55. 2000..The exploitation of auto-orientation of magnetic anisotropic metalloproteins represents a step ahead in the investigation of the conformational space of peripheral residues that are not fixed by the protein folding... - Heme methyl 1H chemical shifts as structural parameters in some low-spin ferriheme proteinsI Bertini
Center for Magnetic Resonance, Department of Chemistry, University of Florence, Italy
J Biol Inorg Chem 4:515-9. 1999..Therefore, by taking advantage of this study, information on the position of the axial ligands, that can be used as a constraint for structure determination, can be obtained from the shifts of the methyl protons... - 15N chemical shift changes in cytochrome b5: redox-dependent vs. guanidinium chloride-induced changesI Bertini
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
J Biol Inorg Chem 5:761-4. 2000..It is concluded that changes in hydrogen bonding upon reduction must be modest and cannot account for the observed chemical shift effects. Alternative explanations should thus be looked for... - Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMRI Bertini
Department of Chemistry, Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Florence, 50019 Sesto Fiorentino, Italy
J Magn Reson 147:1-8. 2000..The identification of hydrophilic regions and detection of three long-lived water molecules settles some ambiguities and provides a better representation of the water-protein interactions in oxidized cytochrome c... - Browsing gene banks for Fe2S2 ferredoxins and structural modeling of 88 plant-type sequences: an analysis of fold and functionIvano Bertini
Centro di Risonanze Magnetiche, University of Florence, Sesto Fiorentino, Italy
Proteins 46:110-27. 2002.... - Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1F Arnesano
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
Biochemistry 40:1528-39. 2001..L., Hou, M. Y., Wernimont, A. K., Pufahl, R. A., and O'Halloran, T. V. (1999) Structure 7, 605-617] provides insights into the copper transfer mechanism, and a pivotal role for Lys65 in the metal capture and release process is proposed... - Copper trafficking: the solution structure of Bacillus subtilis CopZL Banci
Centro di Risonanze Magnetiche and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 40:15660-8. 2001..The nature and the location of conserved residues around the metal-binding site are discussed with respect to their relevance for the metal-binding process. Proposals for the role of CopZ are also presented... - The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMRL Banci
Department of Chemistry, University of Florence, Italy
Biochemistry 34:206-19. 1995..These values compare well with those for diamagnetic proteins of the same size. The solution structure is discussed in the light of the available structural information from X-ray data... - Backbone dynamics of plastocyanin in both oxidation states. Solution structure of the reduced form and comparison with the oxidized stateI Bertini
Magnetic Resonance Center and Department of Chemistry, University of Florence, Via L Sacconi, 6 50019 Sesto Fiorentino, Italy
J Biol Chem 276:47217-26. 2001..The present characterization provides information on both the structural and dynamic behavior of blue copper proteins in solution that is useful to understand further the role(s) of protein dynamics in electron transfer processes... - Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: comparison with the solution structure of the wild-type proteinD Bentrop
Department of Chemistry, University of Florence, Italy
Biochemistry 35:5928-36. 1996..Capillary electrophoresis experiments demonstrate coordination of Ser-77 as an anion. Serine versus cysteine coordination in iron-sulfur proteins is briefly discussed... - (15)N backbone dynamics of ferricytochrome b(562): comparison with the reduced protein and the R98C variantM Assfalg
Magnetic Resonance Center and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
Biochemistry 40:12761-71. 2001..It appears that the increased protein stability of the variant, established previously, is not correlated with an increase in rigidity... - Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?L Banci
Department of Chemistry, University of Florence, Italy
Biochemistry 37:11780-91. 1998..The hydrogen atom which binds the histidine nitrogen detached from copper(I) is structurally identified... - Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded statesL Banci
Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence, 50019, Italy
J Biol Chem 276:8415-26. 2001..These results open new mechanistic aspects of copper transporter domains with physiological copper donor and acceptor proteins... - The solution structure of oxidized Escherichia coli cytochrome b562F Arnesano
Department of Chemistry, Centro di Risonanze Magnetiche, University of Florence, Italy
Biochemistry 38:8657-70. 1999..Quite intriguing is the comparison of the structure of cytochrome b562 with the available structures of cytochromes c' which display a similar folding motif and similar pKa values but very little sequence similarity... - The solution structure of oxidized rat microsomal cytochrome b5F Arnesano
Department of Chemistry, University of Florence, Italy
Biochemistry 37:173-84. 1998..This observation could suggest that, to optimize the electron transfer process, the local mobility should be properly tuned... - Solution structure of reduced microsomal rat cytochrome b5L Banci
Department of Chemistry, University of Florence, Italy
Eur J Biochem 249:270-9. 1997..The structural features in solution of the residues proposed to be involved in protein-protein recognition are found to be largely conserved with respect to the solid state... - ePHOGSY experiments on a paramagnetic protein: location of the catalytic water molecule in the heme crevice of the oxidized form of horse heart cytochrome cI Bertini
Department of Chemistry, University of Florence, Italy
FEBS Lett 415:45-8. 1997..The resulting picture is that there is a detectable movement of the water molecule upon oxidation... - Solution structure calculations through self-orientation in a magnetic field of a cerium(III) substituted calcium-binding proteinI Bertini
Department of Chemistry, University of Florence, Via Gino Capponi 9, Florence, 50121, Italy
J Magn Reson 148:23-30. 2001..This paper shows that Ce(III), like low-spin Fe(III) in hemoproteins, is sufficiently magnetically anisotropic to induce self-orientation to an extent which can be exploited for solution structure determination... - Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced speciesI Bertini
Department of Chemistry, University of Florence, Italy
Biochemistry 34:9851-8. 1995..This is the first time that independently determined solution structures of two redox states of a paramagnetic protein are available. Differences between them and the X-ray structure are discussed... - Characterization of a partially unfolded high potential iron proteinI Bertini
Department of Chemistry, University of Florence, via Gino Capponi, 7, 50121 Florence, Italy
Biochemistry 36:9332-9. 1997.... - Side chain mobility as monitored by CH-CH cross correlation: the example of cytochrome b5L Banci
Magnetic Resonance Center (CERM, University of Florence, Sesto Fiorentino, Italy
J Biomol NMR 20:1-10. 2001..The general pattern is the same for the oxidized and reduced species, indicating that any oxidation-dependent property detected for backbone NH moieties does not affect the CH2 mobility... - The unfolding of oxidized c-type cytochromes: the instructive case of Bacillus pasteuriiIlaria Bartalesi
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Mol Biol 321:693-701. 2002..It is concluded that the thermodynamic stability of the region around the metal cofactor is determined by the chemical nature of the residues around the axial methionine residue... - Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assemblyErica Balatri
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
Structure 11:1431-43. 2003..The availability of the structure has allowed us to model the homologs Sco1 and Sco2 from S. cerevisiae and to discuss the physiological role of the Sco family... - Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7ALucia Banci
Magnetic Resonance Center, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 43:3396-403. 2004..A comparison with metallochaperones and soluble domains of P-type ATPases allows us to relate the primary structure to the occurrence of structural rearrangements upon copper binding... - Solution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogeneous binding of the hemeL Banci
Department of Chemistry and Centro di Risonanze Magnetiche, University of Florence, Sesto Fiorentino, Italy
Eur J Biochem 267:755-66. 2000..Hydrophobic and steric interactions are the key factors in determining the relative stability of one isomer with respect to the other... - The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisitedM Ferraroni
Department of Chemistry, University of Florence, Via Gino Capponi 9, Florence, I 50121, Italy
J Mol Biol 288:413-26. 1999..These properties of the structure have allowed us to revisit the enzymatic mechanism... - Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPaseF Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy
J Biol Chem 276:41365-76. 2001..The analogous mobility of Ccc2a in both Cu(I) and apo forms is reduced with respect to Atx1. Such an adduct is relevant as a structural and kinetic model for copper transfer from Atx1 to Ccc2a in physiological conditions... - Magnetic susceptibility tensor anisotropies for a lanthanide ion series in a fixed protein matrixI Bertini
Department of Chemistry, University of Florence, Via Gino Capponi 9, 50121, Florence, Italy
J Am Chem Soc 123:4181-8. 2001..A knowledge of magnetic susceptibility anisotropy properties of lanthanides is essential in determining the self-orienting properties of lanthanide complexes in solution when immersed in magnetic fields... - The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transductionFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Biol Chem 278:45999-6006. 2003..This similarity suggests an intriguing role of CutA1 proteins in signal transduction through allosteric communications between subunits... - Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidaseLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino 50019, Florence, Italy
J Biol Chem 279:34833-9. 2004..The present results advance the knowledge on the poorly understood molecular aspects of cytochrome c oxidase assembly... - Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solutionLucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Chem 280:35815-21. 2005..We have here also established that the two free cysteines (6 and 111) do not play a role in this behavior... - Protein stability and mutations in the axial methionine loop of a minimal cytochrome cIlaria Bartalesi
Magnetic Resonance Center, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Inorg Chem 9:600-8. 2004..While the structure remains essentially the same, the stability decreases with mutations. The comparison with mitochondrial c-type cytochromes is instructive... - Solution structure of apo CopZ from Bacillus subtilis: further analysis of the changes associated with the presence of copperLucia Banci
Department of Chemistry and Centro di Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
Biochemistry 42:13422-8. 2003..It is also shown that copper(I) exchanges among apo CopZ molecules in slow exchange on the NMR time scale, whereas it is known that such exchange between partner molecules (i.e., metallochaperones and metal pumps) is fast... - 15N-1H Residual dipolar coupling analysis of native and alkaline-K79A Saccharomyces cerevisiae cytochrome cMichael Assfalg
Magnetic Resonance Center (CERM, University of Florence, 50019 Sesto Fiorentino, Florence, Italy
Biophys J 84:3917-23. 2003..Importantly, this is the first time that mobility has been found through comparison of RDCs with pseudocontact shifts... - A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)Lucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Mol Biol 323:883-97. 2002.... - A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domainsLucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Chem 280:38259-63. 2005..This dependence could constitute the molecular mechanism to trigger copper(I) translocation and/or ATP7A relocalization from the trans-Golgi network to the plasmatic membrane... - Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein foldingLucia Banci
Department of Chemistry and Centro Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 42:9543-53. 2003.... - Solution structure of oxidized horse heart cytochrome cL Banci
Department of Chemistry, University of Florence, Italy
Biochemistry 36:9867-77. 1997..cerevisiae and to previous results... - Dimethyl propionate ester heme-containing cytochrome b5: structure and stabilityL Banci
Magnetic Resonance Center, University of Florence, Italy
J Biol Inorg Chem 6:490-503. 2001..The available data on the reduction potential and the electron transfer rates are discussed on the basis of the present structural data... - Solution structure of the oxidized 2[4Fe-4S] ferredoxin from Clostridium pasteurianumI Bertini
Department of Chemistry, University of Florence, Italy
Eur J Biochem 232:192-205. 1995..pasteurianum ferredoxin family is 78 pm (residues 3-53). Discrepancies in residues 26-28 may arise from the disorder observed in the X-ray structure in that region... - 1H NMR studies of Chromatium vinosum cytochrome c'I Bertini
Department of Chemistry, University of Florence, Firenze, Italy
Arch Biochem Biophys 282:84-90. 1990..Some evidence is provided for conformational flexibilities. Among the oxidized cytochromes c' the present one is capable of binding cyanide, giving rise to a low spin state. The reduced species is a typical high spin iron(II) system... - An NMR study of the 7Fe-8S ferredoxin from Rhodopseudomonas palustris and reinterpretation of data on similar systemsI Bertini
Department of Chemistry, University of Florence, Italy
Biochemistry 36:3570-9. 1997..The NMR signal patterns of [3Fe-4S] clusters in both 3Fe-4S and 7Fe-8S ferredoxins have been discussed, and some correlations are proposed between signal patterns and the primary sequence... - Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosisEric L Shipp
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 42:1890-9. 2003..Alternatively, a motor neuron-specific substrate may bind this region of the protein, leading to deleterious modifications and/or reactions... - Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced formLucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Biol Chem 281:2333-7. 2006..The structure allows us to further discuss the copper loading mechanism in SOD1... - Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processesIlaria Bartalesi
Centro di Risonanze Magnetiche, University of Florence, Sesto Fiorentino, Italy
Biochemistry 42:739-45. 2003..By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes... - Ortholog search of proteins involved in copper delivery to cytochrome C oxidase and functional analysis of paralogs and gene neighbors by genomic contextFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Proteome Res 4:63-70. 2005..By linking the assembly system to the copper uptake system, Sco allows COX to face alternative copper trafficking pathways... - Structural interplay between calcium(II) and copper(II) binding to S100A13 proteinFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 44:6341-4. 2005 - Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbuminIrfan Baig
Magnetic Resonance Centre and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 43:5562-73. 2004..0 A resolution. All differences are related to local changes in the amino acidic composition... - Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded statesLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Florence, Sesto Fiorentino, 50019, Italy
J Mol Biol 317:415-29. 2002.... - Understanding copper trafficking in bacteria: interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilisLucia Banci
Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino Florence, Italy
Biochemistry 42:1939-49. 2003..Comparing functional data of homologous proteins of other bacteria, it can be concluded that this class of proteins is involved in copper homeostasis but the specific roles are species dependent... - Solution structure of a monoheme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: functional implicationsIlaria Bartalesi
Centro di Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 41:5112-9. 2002..The structures of the others have been modeled by using the available templates and internally validated. Structural similarities in terms of surface properties account for their biophysical features and provide hints about the function... - A 15N NMR mobility study on the dicalcium P43M calbindin D9k and its mono-La3+-substituted formIvano Bertini
Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
Biochemistry 41:5104-11. 2002..They also demonstrate that substitution of a lanthanide ion for calcium, which is a common procedure, does not significantly alter the mobility of the native protein... - Occurrence of copper proteins through the three domains of life: a bioinformatic approachClaudia Andreini
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Proteome Res 7:209-16. 2008..A network involving proteins having roles in both copper transport and respiration was identified, parts or all of which are detected in the majority of the organisms examined... - Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1Lucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 46:9953-62. 2007..These results suggest further that it is the metal-free apo forms of the mutant SOD1 protein that are the agents of its toxicity... - A structural-dynamical characterization of human Cox17Lucia Banci
Magnetic Resonance Center Centro Risonanze Magnetiche CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Biol Chem 283:7912-20. 2008..The copper(I) form of Cox17(2S-S) has features specific for copper chaperones... - Superoxide dismutase folding/unfolding pathway: role of the metal ions in modulating structural and dynamical featuresMichael Assfalg
CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Mol Biol 330:145-58. 2003..4 M, thus demonstrating the importance of metal ions with respect to the unfolding process and protein structure stability. Hints to understand the whole folding process are obtained and discussed... - A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystalLucia Banci
Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto, Florence, Italy
Proc Natl Acad Sci U S A 102:7541-6. 2005..Couples of dimers held by hydrophobic interactions and H bonds are further organized in long chains. The order/disorder transition is discussed in terms of metal binding and physical state... - A quick solution structure determination of the fully oxidized double mutant K9-10A cytochrome c7 from Desulfuromonas acetoxidans and mechanistic implicationsMichael Assfalg
Magnetic Resonance Center and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
J Biomol NMR 22:107-22. 2002..This finding is in agreement with the identification of the protein area around heme IV as the interacting site... - A hint to search for metalloproteins in gene banksClaudia Andreini
Magnetic Resonance Center (CERM, University of Florence, Italy
Bioinformatics 20:1373-80. 2004..SUPPLEMENTARY INFORMATION: A table reporting statistics on the MBP identified; a list of all hits retrieved for the four organisms considered; a figure showing the number of hits for the four organisms as a function of I(d)(Global)... - Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilisLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Biol Chem 278:50506-13. 2003.... - Solution structure and characterization of the heme chaperone CcmEFabio Arnesano
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
Biochemistry 41:13587-94. 2002..The data available suggest that the heme transfer process is likely to involve a heterooligomeric protein complex and occur under a tight enzymatic control... - Paramagnetically induced residual dipolar couplings for solution structure determination of lanthanide binding proteinsRenato Barbieri
Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Am Chem Soc 124:5581-7. 2002..The effect of mobility is also assessed. In principle, information on the mobility can be obtained with a number of lanthanide ions >5, or by combining a smaller number of lanthanide ions with a few orienting devices... - Zinc through the three domains of lifeClaudia Andreini
Magnetic Resonance Center (CERM, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
J Proteome Res 5:3173-8. 2006..8%) is significantly higher than that observed in Bacteria and Archaea (from 5% to 6%). Most of this enrichment is due to the larger portfolio of regulatory proteins in Eukaryota... - Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper bindingFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy
Structure 13:713-22. 2005..This form of the protein is oligomeric. These properties are framed within a complete model of mitochondrial import and COX assembly... - Solution structures of the actuator domain of ATP7A and ATP7B, the Menkes and Wilson disease proteinsLucia Banci
Magnetic Resonance Center CERM University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 48:7849-55. 2009.... - NMR structural analysis of cadmium sensing by winged helix repressor CmtRLucia Banci
Department of Chemistry and Centro Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, Florence 50019, Italy
J Biol Chem 282:30181-8. 2007..Cadmium binding across the dimer interface impairs DNA association by excluding the apo-conformers suited to bind DNA... - Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasisFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Sesto Fiorentino, Florence, Italy
Structure 10:1337-47. 2002..The present structure represents a link between copper-trafficking proteins and cupredoxins. Within a structural and genomic analysis, the role of CopC in copper trafficking is discussed...