An integrated biophysical approach to discovering mechanisms of NDM-1 inhibition for several thiol-containing drugs.

Due to the rapid proliferation of antibiotic-resistant pathogenic bacteria, known as carbapenem-resistant enterobacteriaceae, the efficacy of β-lactam antibiotics is threatened. β-lactam antibiotics constitute over 50% of the available antibiotic arsenal. Recent efforts have been focused on developing inhibitors to these enzymes.

Electrochemical benzylic oxidation of C-H bonds.

Oxidized products have become increasingly valuable as building blocks for a wide variety of different processes and fine chemistry, especially in the benzylic position. We report herein a sustainable protocol for this transformation through C-H functionalization and is performed using electrochemistry as the main power source and tert-butyl hydroperoxide as the radical source for the C-H abstraction. The temperature conditions reported here do not increase above 50 °C and use an aqueous-based medium.

A Noncanonical Metal Center Drives the Activity of the Sediminispirochaeta smaragdinae Metallo-β-lactamase SPS-1.

In an effort to evaluate whether a recently reported putative metallo-β-lactamase (MβL) contains a novel MβL active site, SPS-1 from Sediminispirochaeta smaragdinae was overexpressed, purified, and characterized using spectroscopic and crystallographic studies. Metal analyses demonstrate that recombinant SPS-1 binds nearly 2 equiv of Zn(II), and steady-state kinetic studies show that the enzyme hydrolyzes carbapenems and certain cephalosporins but not β-lactam substrates with bulky substituents at the 6/7 position. Spectroscopic studies of Co(II)-substituted SPS-1 suggest a novel metal center in SPS-1, with a reduced level of spin coupling between the metal ions and a novel Zn metal binding site.

Using PyMOL to Explore the Effects of pH on Noncovalent Interactions between Immunoglobulin G and Protein A: A Guided-Inquiry Biochemistry Activity.

Students' understandings of foundational concepts such as noncovalent interactions, pH and pK are crucial for success in undergraduate biochemistry courses. We developed a guided-inquiry activity to aid students in making connections between noncovalent interactions and pH/pK . Students explore these concepts by examining the primary and tertiary structures of immunoglobulin G (IgG) and Protein A.

Biochemistry students' ideas about how an enzyme interacts with a substrate.

Enzyme-substrate interactions are a fundamental concept of biochemistry that is built upon throughout multiple biochemistry courses. Central to understanding enzyme-substrate interactions is specific knowledge of exactly how an enzyme and substrate interact. Within this narrower topic, students must understand the various binding sites on an enzyme and be able to reason from simplistic lock and key or induced fit models to the more complex energetics model of transition state theory.

Biochemistry students' ideas about shape and charge in enzyme-substrate interactions.

Biochemistry is a visual discipline that requires students to develop an understanding of numerous representations. However, there is very little known about what students actually understand about the representations that are used to communicate ideas in biochemistry. This study investigated biochemistry students' understanding of multiple representations of enzyme-substrate interactions through both student interviews (N = 25) and responses by a national sample (N = 707) to the Enzyme-Substrate Interactions Concept Inventory.

Development of the enzyme-substrate interactions concept inventory.

Enzyme function is central to student understanding of multiple topics within the biochemistry curriculum. In particular, students must understand how enzymes and substrates interact with one another. This manuscript describes the development of a 15-item Enzyme-Substrate Interactions Concept Inventory (ESICI) that measures student understanding of enzyme-substrate interactions.

A guided inquiry experiment for the measurement of activation energies in the biophysical chemistry laboratory: Decarboxylation of pyrrole-2-carboxylate.

A laboratory experiment for undergraduate biophysical chemistry is described, in which the acid concentration and temperature dependences of the decarboxylation of pyrrole-2-carboxylate are measured using a continuous ultraviolet (UV) spectrophotometric assay. Data collection and analysis are structured using principles of guided inquiry. Data leading to the calculation of multiple rate constants at varying temperatures and acid concentrations can be collected within one laboratory period, using inexpensive reagents and standard instrumentation.