Basel researchers merge MHAT chemistry with enzymes, opening new pathways for greener pharmaceutical synthesis.
Chemists have long dreamed of mimicking nature’s precision, and now, thanks to a repurposed enzyme, they’ve taken a leap closer.Researchers at the University of Basel have successfully combined a powerful synthetic method, mixing metal hydride hydrogen atom transfer with enzymatic catalysis to create three-dimensional molecules with unprecedented precision.
The study mark the first time an enzyme has been shown to catalyze this type of reaction, offering a new tool for greener, more selective chemical synthesis.A first-time featCatalysts are essential to modern chemistry, enabling faster, cleaner, and more controlled reactions.Enzymes, the nature’s catalysts, are especially prized for their ability to steer reactions with remarkable specificity and under mild conditions.Yet, their use has been largely limited to biological transformations.MHAT, on the other hand, is a synthetic technique that has gained attention for its ability to turn simple, flat molecules into complex, three-dimensional architectures. These reactions are particularly useful in drug discovery and fine chemical synthesis, where structure determines function.Until now, MHAT chemistry has been dominated by metal-based catalysts operating outside the realm of biology. That has limited its selectivity, particularly in producing molecules in a single chiral form.In drug development, this is a major drawback: mirror-image molecules, known as enantiomers, can have drastically different biological effects. One may be therapeutic, while the other could be inactive or even toxic.To address this, the Basel team turned to nature for inspiration, and tools. Led by Prof. Dr. Thomas R. Ward, the researchers repurposed a haemoprotein, a class of enzymes that naturally contain an iron center.Blueprint for designer catalystsBy subtly engineering its catalytic site, they enabled the enzyme to carry out the MHAT reaction with remarkable stereoselectivity. In test reactions, the enzyme generated the desired enantiomer in ratios as high as 98:2, far outperforming conventional chemical approaches.“Until now, no enzyme that could carry out such a MHAT reaction was known,” said first author Dr. Xiang Zhang. “This is a completely new capability in biocatalysis.”The research is part of the National Center of Competence in Research “Molecular Systems Engineering,” which focuses on integrating biological components into synthetic systems.The work opens new doors for the production of pharmaceuticals and other high-value chemicals using a more sustainable and scalable approach.However, the new method isn’t without challenges. The engineered enzyme is highly specific, meaning it performs well with a narrow range of starting materials.If the structure of the starting molecule changes significantly, the enzyme may need to be redesigned, an effort that takes time and expertise. Moreover, the researchers are still searching for more environmentally friendly ways to produce the metal hydride catalysts used in the reaction.Still, the ability to combine the precision of enzymes with the versatility of synthetic chemistry represents a powerful new chapter for green chemistry.By blurring the lines between biology and chemistry, scientists may be closer than ever to building complex molecules elegantly, efficiently, and with purpose just like nature.The findings have been published in the journal Nature.
Metal Hydride Hydrogen Atom Transfer MHAT Molecules Pharmaceutical Synthesis University Of Basel
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