Professor Rebecca Goss FRSC
Winner: 2022 Corday-Morgan Prize
University of St Andrews
For pioneering the use of enzymatic halogenation/cross-coupling in C‒H activation.
Celebrate Professor Rebecca Goss
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More than 90% of pharmaceuticals are manufactured using a process called halogenation which bonds carbon to a halogen (typically chlorine, bromine or iodine) – called a C–X bond. More than 20%, including drugs such as Claritin, retain this halogen (X-factor) in the final product; it gives the drug its activity and makes sure that it is properly processed by the body. Drugs containing this X-factor are used to treat medical conditions such as cancer, diabetes, high cholesterol, stomach ulcers, anaemia, asthma, epilepsy, and others.
Whilst the ability to selectively make C–X bonds is essential, current chemical halogenation methods to achieve this are inefficient, expensive and require toxic chemicals, with significant supply chain fragility. Current processes are often accompanied by poor selectivity, which results in unspecific halogenation and undesired by-products, creating difficulties in the downstream purification process and environmentally detrimental waste.
Professor Goss and her team use cheap, easy to handle and readily available salt (nothing more than common table or sea salt), and, with an enzyme, can precision edit even quite complicated molecules, to add in a C–X bond. They have found a way of mining for new enzymes, searching uncharted gene sequences directly – a little like a ’word search’. Their approach can, for the first time, be used to directly reveal C–X forming enzymes. A C–X bond is like a gateway to access almost any other chemical substitution. In this way, the team can use their halogenase enzymes for C–H activation and diversification.
Using these enzymes in parallel with the mild aqueous conditions that the team have developed, they can selectively change a C–H bond into C–almost anything. And they can develop these reactions so that they work even in a living cell.
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