Research Topics
Genomes and Genes | I BertiniSummaryAffiliation: University of Florence Country: Italy Publications
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Publications
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...- High-resolution characterization of intrinsic disorder in proteins: expanding the suite of (13)C-detected NMR spectroscopy experiments to determine key observablesIvano Bertini
CERM University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Chembiochem 12:2347-52. 2011..The test was performed on the yeast Cox17 protein, known to gain its function through maturation from an intrinsically disordered state (see figure)... - On the use of ultracentrifugal devices for sedimented solute NMRIvano Bertini
Center for Magnetic Resonance CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, FI, Italy
J Biomol NMR 54:123-7. 2012..We designed two different devices and we here report the directions for using such devices and the relevant equations for determining the parameters for sedimentation... 
MaxOcc: a web portal for maximum occurrence analysisIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, FI, Italy
J Biomol NMR 53:271-80. 2012..cerm.unifi.it/access/index/maxocc . It can be used freely upon registration to the grid with a digital certificate...- Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteinsIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino FI, Italy
Phys Chem Chem Phys 14:9149-56. 2012..The data, acquired at 298 K and at 278 K, suggest that compact conformations are disfavoured by decreasing the temperature... - Structural insights into the ferroxidase site of ferritins from higher eukaryotesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, 50019 Sesto Fiorentino, Florence, Italy
J Am Chem Soc 134:6169-76. 2012..Here two different di-iron species are trapped in the active site, with intermetal distances corresponding to those of the ferric dimer in crystal 1 and of the dicopper centers and corresponding rearrangement of the His54 side chain... - The catalytic domain of MMP-1 studied through tagged lanthanidesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Sacconi 6, 50019 Sesto Fiorentino, Italy
FEBS Lett 586:557-67. 2012.... - Metabolomic NMR fingerprinting to identify and predict survival of patients with metastatic colorectal cancerIvano Bertini
CERM and Department of Chemistry, University of Florence, Florence, Italy
Cancer Res 72:356-64. 2012..Our findings establish that (1)H-NMR profiling of patient serum can provide a strong metabolomic signature of mCRC and that analysis of this signature may offer an independent tool to predict OS... - Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examplesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 131:5134-44. 2009.... - Solution structure and dynamics of S100A5 in the apo and Ca2+-bound statesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Inorg Chem 14:1097-107. 2009.... 
Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)Ivano Bertini
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
J Biol Chem 284:12821-8. 2009....- Perspectives in paramagnetic NMR of metalloproteinsIvano Bertini
Magnetic Resonance Center, University of Florence, Via L Sacconi 6, 50019, Sesto Fiorentino, FI, Italy
Dalton Trans . 2008.... - Intra- and interdomain flexibility in matrix metalloproteinases: functional aspects and drug designIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Curr Pharm Des 15:3592-605. 2009..The implications of the observed intra- and interdomain flexibility in matrix metalloproteinases for drug design have been analyzed and discussed... - Ultrafast MAS solid-state NMR permits extensive 13C and 1H detection in paramagnetic metalloproteinsIvano Bertini
Magnetic Resonance Center, CERM, University of Florence, Sesto Fiorentino, Italy
J Am Chem Soc 132:5558-9. 2010..Furthermore, using the known crystal structure of the compound, we are able to distinguish and measure pseudocontact (PCS) contributions to the shifts up to the coordinating ligands and to unveil structural information... - NMR properties of sedimented solutesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Sesto Fiorentino FI, Italy
Phys Chem Chem Phys 14:439-47. 2012..The latter possibility opens new horizons for NMR of sedimented systems... - Conformational space of flexible biological macromolecules from average dataIvano Bertini
CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 132:13553-8. 2010..The computer program is publicly available using the grid computing infrastructure through the authors' Web portal... - Solid-state NMR of proteins sedimented by ultracentrifugationIvano Bertini
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 108:10396-9. 2011..NMR of transiently sedimented molecules under fast magic angle spinning has the advantage of overcoming protein size limitations of solution NMR without the need of sample crystallization/precipitation required by solid-state NMR... - A new structural model of Aβ40 fibrilsIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 133:16013-22. 2011..The revealed structural diversity in Aβ fibrils points to a complex picture of Aβ fibrillation... - A Grid-enabled web portal for NMR structure refinement with AMBERIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, Italy
Bioinformatics 27:2384-90. 2011..This refinement however presents various subtleties, from the proper formatting of conformational restraints to the definition of suitable protocols... - 13C direct-detection biomolecular NMR spectroscopy in living cellsIvano Bertini
CERM and Department of Chemistry Ugo Schiff, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
Angew Chem Int Ed Engl 50:2339-41. 2011 - Principles and patterns in the interaction between mono-heme cytochrome c and its partners in electron transfer processesIvano Bertini
Magnetic Resonance Center, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Metallomics 3:354-62. 2011.... - Menkes diseaseI Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019, Sesto Fiorentino, Italy
Cell Mol Life Sci 65:89-91. 2008..The mechanism for sensing the concentration of copper, for trafficking, as well as the details of the mechanism of copper translocation across the membrane are unknown... - Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12Ivano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 130:7011-21. 2008..Hints on the probable conformations are also obtained. This experimental finding opens new perspectives for the often hypothesized active role of the hemopexin-like domain in the enzymatic activity of MMPs... - Mapping protein-protein interaction by 13C'-detected heteronuclear NMR spectroscopyIvano Bertini
Department of Chemistry, University of Florence, 50019, Sesto Fiorentino, Italy
J Biomol NMR 36:111-22. 2006..It is here proposed that protonless (13)C direct-detection NMR is a useful complement to (1)H based NMR spectroscopy for monitoring protein-protein and protein-ligand interactions... - Monomorphism of human cytochrome cIvano Bertini
Magnetic Resonance Center, University of Florence, 50019 Sesto Fiorentino, Italy
Genomics 88:669-72. 2006..Surprisingly, none of the putative SNPs survived experimental validation. We conclude that non-rare allelic variants of the Cyt c protein are absent in the human populations analyzed in this study... - Towards a protocol for solution structure determination of copper(II) proteins: the case of Cu(II)Zn(II) superoxide dismutaseIvano Bertini
CERM and Department of Chemistry, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Chembiochem 8:1422-9. 2007..1H NOEs and 1H and 13C R1 data are sufficient to produce a good/reasonable solution structure, as demonstrated for a monomeric species of superoxide dismutase, a 153-residue protein... - Protonless 13C direct detection NMR: characterization of the 37 kDa trimeric protein CutA1Ivano Bertini
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
Proteins 70:1196-205. 2008..The structural and dynamical knowledge obtained for this system may contribute to understand its biological role... - Evolution of mitochondrial-type cytochrome c domains and of the protein machinery for their assemblyIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Inorg Biochem 101:1798-811. 2007..Archaea have inherited from Bacteria system I or, possibly, an evolutionary intermediate between system II and system I... - Snapshots of the reaction mechanism of matrix metalloproteinasesIvano Bertini
Magnetic Resonance Center (CERM, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 45:7952-5. 2006 - Asymmetry in 13C-13C COSY spectra provides information on ligand geometry in paramagnetic proteinsIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Am Chem Soc 127:12216-7. 2005..The monodentate or bidentate metal binding mode of carboxylates was identified directly via NMR... - NMR spectroscopy of paramagnetic metalloproteinsIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Chembiochem 6:1536-49. 2005..Finally, a section is dedicated to the significant progress made on 13C direct detection, which reduces the negative effects of paramagnetism and may constitute a new chapter in the whole field of NMR spectroscopy... - Paramagnetic metal ions in ligand screening: the Co(II) matrix metalloproteinase 12Ivano Bertini
Magnetic Resonance Center, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 43:2254-6. 2004 - Exploring the subtleties of drug-receptor interactions: the case of matrix metalloproteinasesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 129:2466-75. 2007.... - Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domainsIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Am Chem Soc 129:12786-94. 2007..Such variety is somewhat reduced in the calmodulin-alpha-synuclein adduct, which however still retains high flexibility. The flexibility of the calmodulin-alpha-synuclein adduct is an unexpected result of this research... - Metals in the "omics" world: copper homeostasis and cytochrome c oxidase assembly in a new lightIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Biol Inorg Chem 13:3-14. 2008..The long-term goal of this approach is the overall description of how metals are framed as essential factors within living cells, which in fact is the ultimate purpose of bioinorganic chemistry... - 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... - 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... - 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.... - 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... - 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... - 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 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... - 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... - 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... - 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... - 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... - 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 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 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... - 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... - 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... - 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 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... - 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... - 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.... - 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... - 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 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.... - 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 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... - 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.... - 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... - 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... - 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... - 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... - 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... - 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 - 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... - 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... - 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... - 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... - 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... - 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.... - 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... - 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... - 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... - 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... - Paramagnetic NMR analysis of the seven-iron ferredoxin from the hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals structural similarity to other dicluster ferredoxinsD Bentrop
Department of Chemistry, University of Florence, Italy
Eur J Biochem 236:92-9. 1996..The C alpha-C beta-S-Fe dihedral angles of the cysteine residues coordinating the four-iron cluster could be estimated, and the electronic structure of the three-iron cluster is discussed... - 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... - 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... - 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... - 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 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... - 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... - 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.... - 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)... - 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... - 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... - The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonanceL Banci
Department of Chemistry, University of Florence, Italy
Eur J Biochem 225:715-25. 1994..We do not know of any previous determination of the structure of a paramagnetic protein in solution by NMR. The effect of paramagnetism on the quality of the structure determination is discussed... - 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... - NOE and two-dimensional correlated 1H-NMR spectroscopy of cytochrome c' from Chromatium vinosumL Banci
Department of Chemistry, University of Florence, Italy
Eur J Biochem 204:107-12. 1992..This assignment has rationalized on a sound basis the biochemical behavior of this protein with pH and has showed the utility of this kind of spectroscopy for the other cytochromes c' structures and analogous systems... - 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... - 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... - Paramagnetic relaxation as a tool for solution structure determination: Clostridium pasteurianum ferredoxin as an exampleI Bertini
Department of Chemistry, University of Florence, Firenze, Italy
Proteins 29:348-58. 1997.... - 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... - X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ionLucia Banci
Centro di Risonanze Magnetiche and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
Biochemistry 42:2467-74. 2003..These results are instructive and have been discussed with respect to the molecular basis of copper trafficking... - 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...