S
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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Journal ArticleDOI
Biogeochemical processes and geotechnical applications: progress, opportunities and challenges
Jason T. DeJong,Kenichi Soga,Edward Kavazanjian,Susan E. Burns,L.A. van Paassen,A. Al Qabany,Ahmet H. Aydilek,Sookie S. Bang,Malcolm Burbank,Laurie F. Caslake,Chien-Yen Chen,X. Cheng,Jian Chu,Stefano Ciurli,A. Esnault-Filet,Suzanne Fauriel,Nasser Hamdan,Toshiro Hata,Y. Inagaki,Stephan A. Jefferis,M. Kuo,Lyesse Laloui,Joan M. Larrahondo,David A. C. Manning,Brian C. Martinez,Brina M. Montoya,Douglas C. Nelson,Angelica M. Palomino,Philip Renforth,J. C. Santamarina,Eric A. Seagren,Burak F. Tanyu,Michael Tsesarsky,Thomas J. Weaver +33 more
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.
Stefano Benini,Wojciech Rypniewski,Keith S. Wilson,Silvia Miletti,Stefano Ciurli,Stefano Mangani +5 more
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
Stefano Ciurli,Stefano Benini,Wojciech Rypniewski,Keith S. Wilson,Silvia Miletti,Stefano Mangani +5 more
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.