M. Piccioli

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Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila.

I. Bertini, C. Luchinat, I. Felli, 1994, European journal of biochemistry.

Mapping the interaction between the hemophore HasA and its outer membrane receptor HasR using CRINEPT-TROSY NMR spectroscopy.

M. Delepierre, I. Bertini, P. Turano, 2009, Journal of the American Chemical Society.

13C direct detected COCO-TOCSY: a tool for sequence specific assignment and structure determination in protonless NMR experiments.

M. Piccioli, S. Balayssac, B. Jiménez, 2006, Journal of magnetic resonance.

Tailored HCCH-TOCSY experiment for resonance assignment in the proximity of a paramagnetic center.

M. Piccioli, L. Poggi, 2002, Journal of magnetic resonance.

Insights into Interprotein Electron Transfer of Human Cytochrome c Variants Arranged in Multilayer Architectures by Means of an Artificial Silica Nanoparticle Matrix

Marco Allegrozzi, P. Turano, M. Piccioli, 2016, ACS omega.

Transient iron coordination sites in proteins: Exploiting the dual nature of paramagnetic NMR

P. Turano, M. Piccioli, 2015 .

ePHOGSY experiments on a paramagnetic protein: location of the catalytic water molecule in the heme crevice of the oxidized form of horse heart cytochrome c

I. Bertini, C. Luchinat, M. Piccioli, 1997, FEBS letters.

Paramagnetic NMR Spectroscopy Is a Tool to Address Reactivity, Structure, and Protein–Protein Interactions of Metalloproteins: The Case of Iron–Sulfur Proteins

M. Piccioli, 2020, Magnetochemistry.

13C-detected protonless NMR spectroscopy of proteins in solution

Ivano Bertini, Wolfgang Bermel, Roberta Pierattelli, 2006 .

Sequence-specific assignments in NMR spectra of paramagnetic systems: A non-systematic approach

M. Piccioli, R. Louro, F. Cantini, 2021, Inorganica Chimica Acta.

The long-standing relationship between paramagnetic NMR and iron–sulfur proteins: the mitoNEET example. An old method for new stories or the other way around?

L. Banci, M. Piccioli, A. Gallo, 2021, Magnetic resonance.

The IR-15N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules

M. Piccioli, S. Ciofi‐Baffoni, Riccardo Muzzioli, 2014, Journal of biomolecular NMR.

The solution structure of the monomeric copper, zinc superoxide dismutase from Salmonella enterica: structural insights to understand the evolution toward the dimeric structure.

M. Piccioli, A. Battistoni, M. Sette, 2008, Biochemistry.

NMR assignment of reduced form of copper, zinc superoxide dismutase from Salmonella enterica

M. Piccioli, A. Battistoni, M. Sette, 2007, Biomolecular NMR assignments.

Structural and dynamical properties of a partially unfolded Fe4S4 protein: role of the cofactor in protein folding.

A. Rosato, I. Bertini, C. Luchinat, 1999, Biochemistry.

Assignment Strategy for Fast Relaxing Signals: Complete Aminoacid Identification in Thulium Substituted Calbindin D9K

M. Piccioli, S. Balayssac, B. Jiménez, 2006, Journal of biomolecular NMR.

Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools

C. Spronk, S. Ciurli, F. Musiani, 2018, JBIC Journal of Biological Inorganic Chemistry.

A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase

I. Bertini, M. Piccioli, M. Viezzoli, 2005, European Biophysics Journal.

1H NMR investigation of reduced copper-cobalt superoxide dismutase

I. Bertini, M. Piccioli, M. Viezzoli, 2004, European Biophysics Journal.

Copper-zinc superoxide dismutase: A paramagnetic protein that provides a unique frame for the NMR investigation

I. Bertini, C. Luchinat, M. Piccioli, 1994 .

Direct-detected 13C NMR to investigate the iron(III) hemophore HasA.

M. Delepierre, I. Bertini, P. Turano, 2006, Journal of the American Chemical Society.

PRE‐driven protein NMR structures: an alternative approach in highly paramagnetic systems

M. Piccioli, R. Louro, F. Cantini, 2020, The FEBS journal.

NMR of paramagnetic metalloproteins in solution: Ubi venire, quo vadis?

M. Piccioli, R. Louro, F. Cantini, 2022, Journal of inorganic biochemistry.

The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development

S. Ciurli, M. Piccioli, B. Zambelli, 2022, Biomolecules.

The influence of a surface charge on the electronic and steric structure of a high potential iron-sulfur protein

I. Bertini, C. Luchinat, I. Felli, 1996, JBIC Journal of Biological Inorganic Chemistry.

The structure of iron-sulfur clusters in proteins as monitored by NMR, mössbauer, EPR and molecular dynamics

I. Bertini, C. Luchinat, L. Banci, 1993 .

1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.

F. Capozzi, I. Bertini, C. Luchinat, 1993, European journal of biochemistry.

NMR is a unique and necessary step in the investigation of iron sulfur proteins: the HiPIP from R. gelatinosus as an example

F. Capozzi, I. Bertini, C. Luchinat, 1992 .

[4Fe-4S] Cluster Assembly in Mitochondria and Its Impairment by Copper.

E. Novellino, L. Banci, M. Piccioli, 2017, Journal of the American Chemical Society.

Molecular Structure of Cu(II)-Bound Amyloid-β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer’s Disease

M. Piccioli, Andrea Giachetti, S. Ciofi‐Baffoni, 2022, JACS Au.

Measuring transverse relaxation in highly paramagnetic systems

M. Piccioli, R. Louro, F. Cantini, 2020, Journal of Biomolecular NMR.

Spectroscopic studies on Cu2Zn2SOD: a continuous advancement of investigation tools

I. Bertini, C. Luchinat, L. Banci, 1990 .

Paramagnetic NMR spectroscopy of native and cobalt substituted manganese superoxide dismutase from Escherichia coli

M. Piccioli, J. Renault, C. Verchère-Béaur, 1997, FEBS letters.

Paramagnetism-based versus classical constraints: An analysis of the solution structure of Ca Ln calbindin D9k

I. Bertini, C. Luchinat, G. Parigi, 2001, Journal of biomolecular NMR.

Relaxation-based NMR assignment: Spotlights on ligand binding sites in human CISD3.

L. Banci, M. Piccioli, F. Cantini, 2022, Journal of inorganic biochemistry.

Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes.

L. Banci, M. Piccioli, S. Ciofi‐Baffoni, 2019, Journal of molecular biology.

Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase

A. Scozzafava, I. Bertini, C. Luchinat, 1989 .

Transient versus steady state NOE in paramagnetic molecules Cu2Co2SOD as an example

I. Bertini, C. Luchinat, L. Banci, 1990, FEBS letters.

NMR structures of paramagnetic metalloproteins

L. Banci, M. Piccioli, F. Arnesano, 2005, Quarterly Reviews of Biophysics (print).

Copper‐cobalt superoxide dismutase: A re‐examination of the 1H NMR spectrum through a novel selectively deuteriated derivative

A. Scozzafava, I. Bertini, M. Piccioli, 1993 .

ADVANCES IN THE NMR INVESTIGATION OF PARAMAGNETIC MOLECULES IN SOLUTION

A. Scozzafava, L. Banci, M. Piccioli, 1992 .

Assignment of active-site protons in the 1H-NMR spectrum of reduced human Cu/Zn superoxide dismutase.

F. Capozzi, I. Bertini, C. Luchinat, 1991, European journal of biochemistry.

Cobalt(II) as a probe of the metal binding sites of transferrins

M. Piccioli, L. Messori, 1990 .

The role of a conserved tyrosine residue in high‐potential iron sulfur proteins

C. Haynes, I. Felli, M. Piccioli, 1995, Protein science : a publication of the Protein Society.

A simple protocol to study blue copper proteins by NMR.

C. Luchinat, M. Piccioli, L. Poggi, 2003, European journal of biochemistry.

The conformation of biliverdin in dimethyl sulfoxide: implications for the coordination with copper

M. Piccioli, I. Spasojević, M. Žižić, 2019, Structural Chemistry.

Paramagnetic probes in metalloproteins.

I. Bertini, C. Luchinat, M. Piccioli, 2001, Methods in enzymology.

THE THREE DIMENSIONAL STRUCTURE OF THE PARAMAGNETIC PROTEIN HIPIP I FROM E.HALOPHILA THROUGH NUCLEAR MAGNETIC RESONANCE

I. Bertini, C. Luchinat, I. Felli, 1994 .

The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance.

I. Bertini, C. Luchinat, I. Felli, 1994, European journal of biochemistry.

The NMR contribution to protein–protein networking in Fe–S protein maturation

L. Banci, M. Piccioli, S. Ciofi‐Baffoni, 2018, JBIC Journal of Biological Inorganic Chemistry.

The iron-sulfur cluster in the oxidized high-potential iron protein from Ectothiorhodospira halophila

F. Capozzi, I. Bertini, C. Luchinat, 1993 .

Molecular view of an electron transfer process essential for iron–sulfur protein biogenesis

I. Bertini, L. Banci, V. Calderone, 2013, Proceedings of the National Academy of Sciences.

Two‐dimensional 1H NMR spectra of ferricytochrome c 551 from Pseudomonas aeruginosa

M. Piccioli, J. Salgado, J. Moratal, 1993, FEBS letters.

Formation of [4Fe-4S] clusters in the mitochondrial iron-sulfur cluster assembly machinery.

E. Novellino, L. Banci, M. Piccioli, 2014, Journal of the American Chemical Society.

[2Fe-2S] cluster transfer in iron–sulfur protein biogenesis

L. Banci, S. Neri, M. Piccioli, 2014, Proceedings of the National Academy of Sciences.

New Approaches to NMR of Paramagnetic Molecules

C. Luchinat, M. Piccioli, 1995 .

The Solution Structure of Oxidized HiPIP I from Ectothiorhodospira halophila; Can NMR Spectroscopy Be Used to Probe Rearrangements Associated with Electron Transfer Processes?

I. Bertini, C. Luchinat, I. Felli, 1995 .

Solution structure of the oxidized 2[4Fe-4S] ferredoxin from Clostridium pasteurianum.

I. Bertini, C. Luchinat, M. Piccioli, 1995, European journal of biochemistry.

Multiple selective excitation as a tool for NMR studies of paramagnetic metalloproteins

M. Piccioli, N. Goasdoué, Isabelle Correia, 2000 .

Biomolecular NMR at 1.2 GHz

A. Rosato, L. Tenori, C. Luchinat, 2019, 1910.07462.

Kinetic studies on metal removal from transferrins by pyrophosphate. Investigation on iron(III) and manganese(III) derivatives

A. Scozzafava, I. Bertini, C. Luchinat, 1988 .

Conjuring up a ghost: structural and functional characterization of FhuF, a ferric siderophore reductase from E. coli

T. Cordeiro, M. Piccioli, F. Barrière, 2021, JBIC Journal of Biological Inorganic Chemistry.

NOE-less protein structures-an alternative paradigm in Highly Paramagnetic Systems

M. Piccioli, R. Louro, F. Cantini, 2020, 2002.01228.

Mobility Studies in Proteins by 15N Nuclear Magnetic Resonance: Rusticyanin as an Example

M. Piccioli, B. Jiménez, J. Moratal, 2004 .

Folding properties of iron—sulfur proteins

I. Bertini, C. Luchinat, M. Piccioli, 1998 .

Deciphering the Structural Role of Histidine 83 for Heme Binding in Hemophore HasA*

Paola Turano, Mario Piccioli, Anne Lecroisey, 2008, Journal of Biological Chemistry.

The solution structure refinement of the paramagnetic reduced high-potential iron-sulfur protein I from Ectothiorhodospira halophila by using stable isotope labeling and nuclear relaxation.

A. Rosato, I. Bertini, C. Luchinat, 1996, European journal of biochemistry.

NMR of Paramagnetic Proteins: 13C Derived Paramagnetic Relaxation Enhancements Are an Additional Source of Structural Information in Solution

M. Piccioli, R. Louro, F. Cantini, 2023, Magnetochemistry.

Electrochemical nitration of myoglobin at tyrosine 103: structure and stability.

L. Alcaraz, M. Piccioli, V. Montiel, 2013, Archives of biochemistry and biophysics.

Electron self-exchange in high-potential iron-sulfur proteins. Characterization of protein I from Ectothiorhodospira vacuolata.

I. Bertini, C. Luchinat, M. Piccioli, 1993, Biochemistry.

Paramagnetic NMR spectroscopy and coordination structure of cobalt(II) Cys112Asp azurin

Tadashi Mizoguchi, Harry B. Gray, Claudio Luchinat, 1995 .

The iron-sulfur cluster (Fe4S4) centers in ferredoxins studied through proton and carbon hyperfine coupling. Sequence-specific assignments of cysteines in ferredoxins from Clostridium acidi urici and Clostridium pasteurianum

F. Capozzi, I. Bertini, C. Luchinat, 1994 .

The electronic structure of [Fe4S4]3+ clusters in proteins. An investigation of the oxidized high-potential iron-sulfur protein II from Ectothiorhodospira vacuolata.

I. Bertini, C. Luchinat, S. Ciurli, 1993, Biochemistry.

The biogenesis of iron–sulfur proteins: from cellular biology to molecular aspects

M. Piccioli, 2018, JBIC Journal of Biological Inorganic Chemistry.

The Intriguing mitoNEET: Functional and Spectroscopic Properties of a Unique [2Fe-2S] Cluster Coordination Geometry

L. Banci, M. Piccioli, Francesca Camponeschi, 2022, Molecules.

Paramagnetic NMR analysis of the seven-iron ferredoxin from the hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals structural similarity to other dicluster ferredoxins.

J. Mendes, I. Bertini, C. Luchinat, 1996, European journal of biochemistry.

Identification of the iron ions of high potential iron protein from Chromatium vinosum within the protein frame through two-dimensional NMR experiments

F. Capozzi, I. Bertini, C. Luchinat, 1992 .

Hydrogen-1 NOE and ligand field studies of copper-cobalt superoxide dismutase with anions

I. Bertini, C. Luchinat, L. Banci, 1990 .

Cobalt(II)‐ and Nickel(II)‐Substituted Proteins

Lucia Banci, Mario Piccioli, L. Banci, 2007 .

X-ray, NMR and molecular dynamics studies on reduced bovine superoxide dismutase: implications for the mechanism.

I. Bertini, C. Luchinat, P. Carloni, 1994, Biochemical and Biophysical Research Communications - BBRC.

Role of the Iron Axial Ligands of Heme Carrier HasA in Heme Uptake and Release*

M. Delepierre, N. Wolff, P. Turano, 2012, The Journal of Biological Chemistry.

Backbone dynamics of rusticyanin: the high hydrophobicity and rigidity of this blue copper protein is responsible for its thermodynamic properties.

M. Piccioli, B. Jiménez, J. Moratal, 2003, Biochemistry.

Electron self-exchange of cytochrome c measured via13C detected protonless NMR

P. Turano, M. Piccioli, S. Cacciatore, 2013 .

Locating the Metal Ion in Calcium‐Binding Proteins by Using Cerium(III) as a Probe

I. Bertini, C. Luchinat, M. Piccioli, 2001, Chembiochem : a European journal of chemical biology.

Cross correlation rates between Curie spin and dipole-dipole relaxation in paramagnetic proteins: The case of Cerium substituted Calbindin D9k

I. Bertini, C. Luchinat, G. Cavallaro, 2002, Journal of biomolecular NMR.

Radical-SAM dependent nucleotide dehydratase (SAND), rectification of the names of an ancient iron-sulfur enzyme using NC-IUBMB recommendations

H. Stark, W. Hagen, M. Piccioli, 2022, Frontiers in Molecular Biosciences.

The IR-15N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules

M. Piccioli, S. Ciofi‐Baffoni, Riccardo Muzzioli, 2014, Journal of Biomolecular NMR.

13C direct detected NMR increases the detectability of residual dipolar couplings.

Ivano Bertini, Claudio Luchinat, Giacomo Parigi, 2006, Journal of the American Chemical Society.

13C direct detected experiments: optimization for paramagnetic signals.

I. Bertini, M. Piccioli, B. Jiménez, 2005, Journal of magnetic resonance.

The solution structure of oxidized HiPIP I from Echtothiorhodospira halophila. Can NMR probe rearrangements associated to electron transfer processes

I. Bertini, C. Luchinat, I. Felli, 1995 .

Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools

C. Spronk, S. Ciurli, F. Musiani, 2018, JBIC Journal of Biological Inorganic Chemistry.

Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation

Bruno M. Fonseca, M. Piccioli, R. Louro, 2023, Molecules.

Paramagnetic NMR restraints for the characterization of protein structural rearrangements.

C. Luchinat, E. Ravera, G. Parigi, 2023, Current opinion in structural biology.

Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.

I. Bertini, C. Luchinat, M. Piccioli, 2000, Journal of magnetic resonance.

COSY spectra of paramagnetic macromolecules: Observability, scalar effects, cross‐correlation effects, relaxation‐allowed coherence transfer

I. Bertini, C. Luchinat, M. Piccioli, 1994 .

NOE-NOESY, a Further Tool in NMR of Paramagnetic Metalloproteins

I. Bertini, C. Luchinat, M. Piccioli, 1994 .

1H, 13C and 15N assignment of the paramagnetic high potential iron–sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1

M. Piccioli, R. Louro, F. Cantini, 2020, Biomolecular NMR Assignments.

Characterization of a partially unfolded high potential iron protein.

I. Bertini, C. Luchinat, M. Piccioli, 1997, Biochemistry.

The NMR contribution to protein–protein networking in Fe–S protein maturation

L. Banci, M. Piccioli, S. Ciofi‐Baffoni, 2018, JBIC Journal of Biological Inorganic Chemistry.

Correction to: The NMR contribution to protein–protein networking in Fe–S protein maturation

L. Banci, M. Piccioli, S. Ciofi‐Baffoni, 2018, JBIC Journal of Biological Inorganic Chemistry.

Hypothesis: the sound of the individual metabolic phenotype? Acoustic detection of NMR experiments.

Edoardo Saccenti, Stefano Cacciatore, Mario Piccioli, 2015, Omics : a journal of integrative biology.

Development of NMR instrumentation to achieve excitation of large bandwidths in high-resolution spectra at high field.

C. Luchinat, R. Pierattelli, M. Piccioli, 2001, Journal of magnetic resonance.

[4Fe-4S] Cluster Assembly in Mitochondria and Its Impairment by Copper.

E. Novellino, L. Banci, M. Piccioli, 2017, Journal of the American Chemical Society.

Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center

M. Piccioli, R. Louro, F. Cantini, 2023, Journal of Biomolecular NMR.

The structure of a novel ferredoxin – FhuF, a ferric-siderophore reductase from E. coli K-12 with a novel 2Fe-2S cluster coordination

P. Matias, M. Piccioli, R. Louro, 2023, bioRxiv.

New routes to the detection of relaxation allowed coherence transfer in paramagnetic molecules.

M. Piccioli, F. Kateb, 2003, Journal of the American Chemical Society.

C. Luchinat, M. Piccioli, T. Lehmann, 2002, Inorganic chemistry.