Dataset and kinetic model reaction compilation for the radical-induced degradation of formic acid and formate in aqueous solution.

This article contains the individual datasets and complete reaction kinetics compilation for the formic acid/formate component of the kinetic model described in "Radiolytic Degradation of Formic Acid and Formate in Aqueous Solution: Modeling the Final Stages of Organic Mineralization under Advanced Oxidation Process Conditions" [1]. Gamma irradiation data were collected for aqueous sodium formate solutions under pH = 1.5 and 9.

Radiolytic degradation of formic acid and formate in aqueous solution: modeling the final stages of organic mineralization under advanced oxidation process conditions.

The successful use of advanced oxidation processes to treat aqueous solutions containing undesirable organic species requires the degradation of these species to lower molecular weight, lower hazard compounds. Safe application of this technology requires a thorough understanding of the mechanisms of degradation. These oxidative transformations are mainly initiated by the reactions of reactive oxygen species, particularly hydroxyl radicals.

Design and synthesis of potent Gram-negative specific LpxC inhibitors.

Antibiotic resistant hospital acquired infections are on the rise, creating an urgent need for novel bactericidal drugs. Enzymes involved in lipopolysaccharide (LPS) biosynthesis are attractive antibacterial targets since LPS is the major structural component of the outer membrane of Gram-negative bacteria. Lipid A is an essential hydrophobic anchor of LPS and the first committed step in lipid A biosynthesis is catalyzed by a unique zinc dependent metalloamidase, UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC).

Screening for antibacterial inhibitors of the UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) using a high-throughput mass spectrometry assay.

A high-throughput mass spectrometry assay to measure the catalytic activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, LpxC, is described. This reaction is essential in the biosynthesis of lipopolysaccharide (LPS) of gram-negative bacteria and is an attractive target for the development of new antibacterial agents. The assay uses the RapidFire mass spectrometry platform to measure the native LpxC substrate and the reaction product and thereby generates a ratiometric readout with minimal artifacts due to detection interference.

Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus.

Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4'-phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty-acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.