title: Inactivation of urease by catechol: Kinetics and structure.
abstract: Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 1015times higher than the uncatalyzed reaction. Urease is a virulence factor of several human pathogens, in addition to decreasing the efficiency of soil organic nitrogen fertilization. Therefore, efficient urease inhibitors are actively sought. In this study, we describe a molecular characterization of the interaction between urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) with catechol, a model polyphenol. In particular, catechol irreversibly inactivates both SPU and JBU with a complex radical-based autocatalytic multistep mechanism. The crystal structure of the SPU-catechol complex, determined at 1.50Å resolution, reveals the structural details of the enzyme inhibition.
authors.affiliation: Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Italy.
authors.forename: Luca
authors.initials: L
authors.lastname: Mazzei
authors.affiliation: European Molecular Biology Laboratory, DESY, Hamburg, Germany.
authors.forename: Michele
authors.initials: M
authors.lastname: Cianci
authors.affiliation: Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Italy.
authors.forename: Francesco
authors.initials: F
authors.lastname: Musiani
authors.affiliation: Department of Inorganic and Analytical Chemistry, University of Debrecen, Hungary.
authors.forename: Gábor
authors.initials: G
authors.lastname: Lente
authors.affiliation: Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Italy.
authors.forename: Marta
authors.initials: M
authors.lastname: Palombo
authors.affiliation: Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Italy. Electronic address: stefano.ciurli@unibo.it.
authors.forename: Stefano
authors.initials: S
authors.lastname: Ciurli
mesh_terms: D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry; D032449:Canavalia / Q000201:enzymology*; D002396:Catechols / Q000037:antagonists & inhibitors / Q000737:chemistry; D008958:Models, Molecular; D010940:Plant Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry; D058644:Sporosarcina / Q000201:enzymology*; D014510:Urease / Q000037:antagonists & inhibitors / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D002396:Catechols; D010940:Plant Proteins; D014510:Urease; C034221:catechol
keywords: Catechol; Kinetic measurements; Nickel; Urease inhibition; X-ray crystallography