Integrated low emissions cleanup system for coal fueled turbines Phase III bench-scale testing and evaluation

The United States Department of Energy, Morgantown Energy Research Center (DOE/METC), is sponsoring the development of coal-fired turbine technologies such as Pressurized Fluidized Bed Combustion (PFBC), coal Gasification Combined Cycles (GCC), and Direct Coal-Fired Turbines (DCFT). A major technical development challenge remaining for coal-fired turbine systems is high-temperature gas cleaning to meet environmental emissions standards, as well as to ensure acceptable turbine life. The Westinghouse Electric Corporation, Science & Technology Center, has evaluated an Integrated Low Emissions Cleanup (ILEC) concept that has been configured to meet this technical challenge. This ceramic hot gas filter (HGF), ILEC concept controls particulate emissions, while simultaneously contributing to the control of sulfur and alkali vapor contaminants in high-temperature, high-pressure, fuel gases or combustion gases. This document reports on the results of Phase III of the ILEC evaluation program, the final phase of the program. In Phase III, a bench-scale ILEC facility has been tested to (1) confirm the feasibility of the ILEC concept, and (2) to resolve some major filter cake behavior issues identified in PFBC, HGF applications

Competitive Activity-Based Protein Profiling Identifies Aza-β-Lactams as a Versatile Chemotype for Serine Hydrolase Inhibition

Serine hydrolases are one of the largest and most diverse enzyme classes in Nature. Most serine hydrolases lack selective inhibitors, which are valuable probes for assigning functions to these enzymes. We recently discovered a set of aza-β-lactams (ABLs) that act as potent and selective inhibitors of the mammalian serine hydrolase protein-phosphatase methylesterase-1 (PME-1). The ABLs inactivate PME-1 by covalent acylation of the enzyme’s serine nucleophile, suggesting that they could offer a general scaffold for serine hydrolase inhibitor discovery. Here, we have tested this hypothesis by screening ABLs more broadly against cell and tissue proteomes by competitive activity-based protein profiling (ABPP), leading to the discovery of lead inhibitors for several serine hydrolases, including the uncharacterized enzyme α,β-hydrolase domain-containing 10 (ABHD10). ABPP-guided medicinal chemistry yielded a compound ABL303 that potently (IC[subscript 50] ≈ 30 nM) and selectively inactivated ABHD10 in vitro and in living cells. A comparison of optimized inhibitors for PME-1 and ABHD10 indicates that modest structural changes that alter steric bulk can tailor the ABL to selectively react with distinct, distantly related serine hydrolases. Our findings, taken together, designate the ABL as a versatile reactive group for creating first-in-class serine hydrolase inhibitors.National Institutes of Health (U.S.) (Grant GM57034)National Institutes of Health (U.S.) (Postdoctoral Fellowship Grant GM086040)Skaggs Institute for Chemical Biolog