Asymmetric C–H functionalization offers a direct and efficient approach for constructing chiral C–C and C–X bonds, streamlining access to complex molecules. Traditionally, this transformation relies on transition metal catalysis using noble metals such as iridium and rhodium, however their scarcity and high cost limit widespread application. To address these challenges, the Cramer group explored cobalt(III) as a more abundant alternative, demonstrating its potential for asymmetric C–H functionalization.

Proton-coupled electron transfer (PCET) has emerged as a powerful mechanistic framework for driving challenging bond activations in organic synthesis. By coupling proton and electron transfer in a single kinetic step, PCET allows access to reactive radical intermediates under mild conditions that would otherwise require strongly reducing reagents.

Carbon monoxide (CO) poisoning is the leading cause of non-drug-related poisoning in humans, resulting in an estimated 50,000-100,000 emergency room visits and 1,500-2,000 deaths annually in the United States alone.¹ Current treatment options are limited to oxygen administration via normobaric oxygen therapy (NBOT) or hyperbaric oxygen therapy (HBOT), but no point-of-care antidote is available.¹ This talk will focus on recent developments in high affinity CO scavengers that exploit the uniquely strong CO-heme interaction to selectively bind

Pyrrolnitrin (PRN) is a bioactive halometabolite produced from L-tryptophan (L-Trp) through a four-enzyme biosynthetic pathway involving PrnA, PrnB, PrnC, and PrnD. PrnB catalyzes an oxidative ring rearrangement but remains mechanistically unresolved due to the failure to reconstitute activity in vitro. To address this, we examined two PrnB homologs (PsPrnB and FbPrnB) and characterized the binding conformation and affinities of PrnB with two substrates (7-Cl-Trp and Trp) and two substrate analogs (TAM and IDPA).

Thiol dioxygenases (TDOs) are a family of unique non-heme iron-dependent metalloenzymes that catalyze the addition of both atoms of molecular oxygen to the thiol groups of their substrates.¹ Previously characterized members have shown several important roles in thiol and oxygen homeostasis among bacteria, mammals, and plants.² These enzymes belong to the cupin enzyme superfamily, which is characterized by a β-barrel fold and has two semi-conserved cupin binding motifs.

Antioxidant enzymes such as peroxidase, catalase, and superoxide dismutase perform the critical role of converting reactive oxygen species (ROS) like hydrogen peroxide and superoxide into benign molecules such as water and dioxygen. However, some modern cancer treatments seek to take advantage of the destructive effects of ROS to induce cell death in tumor cells¹.