Penn State Chemists Synthesize Enzyme Mimic to Process BTX Chemicals Using Oxygen
Penn State University chemists have developed a synthetic mimic for the oxygen-activating enzyme extradiol dioxygenase, creating a chemical production route that uses oxygen as an input and water as the sole byproduct. Published in the Journal of the American Chemical Society, the research targets the challenging conversion of BTX chemicals—benzene, toluene, and xylenes—by breaking open their extremely stable six-carbon aromatic rings.
Traditional petrochemical manufacturing relies heavily on the unique stabilization property known as aromaticity, where six pi electrons bond in a synergistic arrangement that resists standard reactions. According to Jonathan Kuo, assistant professor of chemistry at Penn State, the newly promoted reaction bypasses this limitation.
“The particular reaction we promoted in this work cannot be performed by any synthetic method, to my knowledge,” Kuo says. “Most reactions that process the BTX chemicals don’t really disturb this arrangement, but the reaction we promoted does. As a result, it becomes possible to convert the BTX chemicals into other families.”
Molecular Design and Iridium Incorporation
Natural oxygen-activating enzymes typically incorporate cobalt, iron, or manganese into their structures. For this synthetic mimic, however, the research team integrated iridium.
This metallic shift improves selectivity against unwanted oxygen side reactions while establishing a framework for longer-lasting synthetic mimics. The team also successfully incorporated specific functional enzymatic features, including a hypothesized functionally important protic residue.
By tailoring the mimic to insert an oxygen atom into the six-carbon aromatic ring, the chemists generate a reactive seven-member ring. This intermediate structure can be cleaved more readily, unlocking diverse chemical building blocks for manufacturing plastics, pharmaceuticals, and other materials.

Chemical Production Implications
Sustainable chemical production faces persistent hurdles in finding reaction routes that eliminate waste and unwanted byproducts. By utilizing oxygen rather than traditional petrochemical processes, the Penn State method offers an alternative pathway for processing feedstocks that are otherwise difficult to alter without destroying the base molecular framework.
The integration of these enzymatic properties into a synthetic iridium-based platform points toward expanded applications in green chemistry.