On June 11, 2025, Rachel Narehood Austin, Diana T. and P. Roy Vagelos Professor of Chemistry, published a new study titled “Benchmarking the Reactivity of Caged Iron(IV)-Oxo Sites within Metal–Organic Frameworks,” which sheds light on a longstanding question in chemistry: what gives certain enzymes in nature their extraordinary catalytic power? Published in the Journal of the American Chemical Society, the research focuses on a fascinating group of proteins known as metalloenzymes, but elucidates their chemistry by using an inorganic surrogate.
The article explores how holding reactants inside confined structures helps metalloenzymes perform essential functions, from breaking down food in our bodies to cleaning up pollutants in the environment. Austin and her co-authors uncover how the balance between the structure that surrounds the metal and the metal itself contributes to its catalytic “superpowers.” By examining how small changes in this environment can dramatically alter the enzyme’s behavior, the team’s findings offer valuable clues about how nature fine-tunes these molecular machines.