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Stefano Ciurli

Researcher at University of Bologna

Publications -  180
Citations -  6909

Stefano Ciurli is an academic researcher from University of Bologna. The author has contributed to research in topics: Urease & Active site. The author has an hindex of 42, co-authored 173 publications receiving 5957 citations. Previous affiliations of Stefano Ciurli include Columbia University & Harvard University.

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Biogeochemical processes and geotechnical applications: progress, opportunities and challenges

TL;DR: In this article, the authors assess the progress, opportunities, and challenges in this emerging field, which consists of a geochemical reaction regulated by subsurface microbiology, including mineral precipitation, gas generation, biofilm formation and biopolymer generation.
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A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels.

TL;DR: The mode of binding of the inhibitor, and a comparison between the native and inhibited urease structures, indicate a novel mechanism for enzymatic urea hydrolysis which reconciles the available structural and biochemical data.
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Nonredox Nickel Enzymes

TL;DR: Crystal structures of inhibitor complexes and mechanisms involving coordination of the enediolate have been proposed, as have mechanisms that involve activatingmetal-bound water molecules to serve as catalytic bases without binding the substrate to the metal.
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Chemistry of Ni2+ in Urease: Sensing, Trafficking, and Catalysis

TL;DR: More recent advances are discussed in the comprehension of the specific role of Ni(2+) in the catalysis and the interplay between Ni( 2+) and other metal ions, such as Zn(2-) and Fe(2+), in the metal-dependent enzyme activity.
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Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms

TL;DR: In this article, a comprehensive critical summary of urease spectroscopy, crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis given to the relationships between the structural features of the Ni-containing active site and the physico-chemical and biochemical properties of this metallo-enzyme.