Researchers at the University of Basel have made a significant stride in chemical synthesis by engineering a natural enzyme to catalyze a difficult chemical reaction. This innovation, detailed in the journal Nature, combines metal hydride hydrogen atom transfer (MHAT) chemistry with enzymatic catalysis, paving the way for environmentally friendly and efficient production of complex molecules, including essential pharmaceuticals and fine chemicals. The core of this development involves modifying a common hemoprotein enzyme to execute MHAT reactions within its active site, enabling the creation of three-dimensional molecules with a specific, single-handed configuration. This precise stereoselectivity, achieving ratios of up to 98:2 for left- to right-handed molecules, is critical for industries like pharmaceuticals, where molecular configuration directly impacts drug efficacy and safety, as underscored by historical cases like thalidomide.
This advancement strongly supports the principles of green chemistry, aiming to reduce environmental impact through minimized hazardous substances, lower energy consumption, and less waste. Enzymes, with their inherent specificity and mild reaction conditions, are central to this approach, reducing reliance on harsh reagents and extreme temperatures. The development of engineered enzymes is a key strategy for making chemical production more sustainable and cost-effective. While the current enzyme shows high specificity, researchers acknowledge that adapting it for different starting materials may require further structural modifications. The team is also investigating more sustainable methods for metal hydride formation to enhance the overall utility of this process. This enzymatic approach is expected to streamline the production of high-value chemicals, offering a cleaner alternative to traditional methods for creating chiral molecules vital for pharmaceuticals and other sectors.