LAUSR

Enzymes are the biological molecules that speed up the rate of chemical reactions in all living organisms from bacteria to the human body through processes called biocatalysis. Naturally occurring organophosphorus hydrolase (OPH) is one example of an enzyme found in several bacteria, a few fungi and cyanobacteria, that has the job of hydrolyzing organophosphates (OPs). Some 40% of the pesticides used worldwide, along with plasticizers, petroleum additives, and chemical warfare agents, are organophosphates. While multiple biotechnological applications across industry such as bioremediation are reliant on OPH, natural enzymes are not sufficiently stable for practical use. In this issue of ACS Central Science, Yuan, Zhu, and co-workers demonstrate, for the first time, a new strategy for an industrially applicable “mimic” for OPH capable of degrading OPs. While nature has evolved over millennia and has optimized enzymatic processes such as those involving OPH, chemists have been busy designing artificial molecules that replicate nature’s exquisite machinery. This “molecular engineering” of sorts is limited only by the creativity and ingenuity of the chemist and their skill in executing synthetic reactions to achieve a desired product. In their work, Yuan, Zhu, and co-workers propose a new strategy for achieving a robust porous artificial enzyme that mimics OPH function. The thermal stability of the artificial enzyme is a key parameter for its practical usage; most naturalmicroorganism enzymes lose their activity as the temperature increases. Central to their design philosophy is replicating the active domain of OPH, which involves two zinc fragments within a 3.3−4.6 Å distance, corresponding to the transition-state barrier crossing and the productrelease steps, as depicted in Figure 1. These next-generation artificial enzymes are affectionately called nanozymes.