Stefano Ciurli

NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.

Molecular characterization of Bacillus pasteurii UreE, a metal-binding chaperone for the assembly of the urease active site.

New insights into the mechanism of purple acid phosphatase through (1)H NMR spectroscopy of the recombinant human enzyme.

Structural basis for the molecular properties of cytochrome c6.

Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD.

Electron transfer from HiPIP to the photooxidized tetraheme cytochrome subunit of Allochromatium vinosum reaction center: new insights from site-directed mutagenesis and computational studies.

Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism.

Preparation and reactivity studies of synthetic microperoxidases containing b-type heme.

Nickel trafficking: insights into the fold and function of UreE, a urease metallochaperone.

UreG, a chaperone in the urease assembly process, is an intrinsically unstructured GTPase that specifically binds Zn2+.

Structure of the intermolecular complex between plastocyanin and cytochrome f from spinach.

High potential iron-sulfur proteins and their role as soluble electron carriers in bacterial photosynthesis: tale of a discovery.

Jack bean (Canavalia ensiformis) urease. Probing acid-base groups of the active site by pH variation.

Low-temperature EPR and Mössbauer spectroscopy of two cytochromes with His-Met axial coordination exhibiting HALS signals.

The nickel site of Bacillus pasteurii UreE, a urease metallo-chaperone, as revealed by metal-binding studies and X-ray absorption spectroscopy.

Intrinsically disordered structure of Bacillus pasteurii UreG as revealed by steady-state and time-resolved fluorescence spectroscopy.

Biochemical studies on Mycobacterium tuberculosis UreG and comparative modeling reveal structural and functional conservation among the bacterial UreG family.

A model-based proposal for the role of UreF as a GTPase-activating protein in the urease active site biosynthesis.

The Ni2+ binding properties of Helicobacter pylori NikR.

High resolution crystal structure of Rubrivivax gelatinosus cytochrome c'.

Zn2+-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation.

High-affinity Ni2+ binding selectively promotes binding of Helicobacter pylori NikR to its target urease promoter.

Structural characterization of binding of Cu(II) to tau protein.

The RNA hydrolysis and the cytokinin binding activities of PR-10 proteins are differently performed by two isoforms of the Pru p 1 peach major allergen and are possibly functionally related.

Helicobacter pylori UreE, a urease accessory protein: specific Ni(2+)- and Zn(2+)-binding properties and interaction with its cognate UreG.

Interaction of selenoprotein W with 14-3-3 proteins: a computational approach.

Zinc inhibition of bacterial cytochrome bc(1) reveals the role of cytochrome b E295 in proton release at the Q(o) site.

Chemistry of Ni2+ in urease: sensing, trafficking, and catalysis.

Model structures of Helicobacter pylori UreD(H) domains: a putative molecular recognition platform.

Holo-Ni2+ Helicobacter pylori NikR contains four square-planar nickel-binding sites at physiological pH.

Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme.

Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni²⁺ and Zn²⁺ reveals a role for the disordered C-terminal arm in metal trafficking.

Unraveling the Helicobacter pylori UreG zinc binding site using X-ray absorption spectroscopy (XAS) and structural modeling.

Metal ion-mediated DNA-protein interactions.

Biochemical and structural studies on native and recombinant Glycine max UreG: a detailed characterization of a plant urease accessory protein.

Intrinsic fluorescence of intrinsically disordered proteins.

Engineered biosealant strains producing inorganic and organic biopolymers.

Denaturant-induced conformational transitions in intrinsically disordered proteins.

The crystal structure of Sporosarcina pasteurii urease in a complex with citrate provides new hints for inhibitor design.

Conformational fluctuations of UreG, an intrinsically disordered enzyme.

Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.

Selectivity of Ni(II) and Zn(II) binding to Sporosarcina pasteurii UreE, a metallochaperone in the urease assembly: a calorimetric and crystallographic study.

Nickel binding properties of Helicobacter pylori UreF, an accessory protein in the nickel-based activation of urease.

FeON-FeOFF: the Helicobacter pylori Fur regulator commutates iron-responsive transcription by discriminative readout of opposed DNA grooves.

Nonredox Nickel Enzymes.

Nickel and human health.