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  Urease and Nickel in Biology Robert P. Hausinger Michigan State University Dia 14 maio | Auditório | 14:30 Abstract Urease, the first enzyme to be crystallized and the first shown to possess nickel, catalyzes a simple reaction, but it requires a remarkably complex biosynthesis machinery. Formation of the dinuclear nickel metallocenter with its bridging carbamylated lysyl ligand is dependent on the functions of the metallochaperone UreE, the GTPase UreG, and the protein scaffold UreF/UreD that contains a molecular tunnel through which nickel must pass. Other nickel-containing enzymes include guanidinase, glyoxylase, acireductone dioxygenase, superoxide dismutase, [NiFe] hydrogenase, carbon monoxide dehydrogenase, acetyl-CoA synthase/decarbonylase, hydroxyacid racemase/epimerase, and methyl coenzyme M reductase. The metallocenters in these enzymes encompass mononuclear and dinuclear sites, more complex clusters, and organometallic complexes, where the biosynthetic pathways for se

  Kerry Hamilton School of Sustainable Engineering and the Built Environment, Arizona State University, USA Kerry Hamilton is an Assistant Professor in the School of Sustainable Engineering and the Built Environment with a joint appointment in the Biodesign Institute Center for Environmental Health Engineering at Arizona State University. She received her doctoral degree in Environmental Engineering from Drexel University and Master’s of Health Science (MHS) degree in Environmental and Occupational Hygiene from Johns Hopkins University. She was a Fulbright Scholar to Australia and Public Health Fellow at the US Environmental Protection Agency. Her research focuses on assessing and reducing health risks from pathogens transmitted by environmental exposures. Frontiers in quantitative risk assessment for antimicrobial resistance (AMR): Modeling contributions from water and wastewater Antimicrobial resistance (AMR) is a critical global issue, with AMR expected to surpass cancer as a l