A light-driven enzymatic enantioselective radical acylation. (https://www.nature.com/articles/s41586-023-06822-x)

These scientists wanted to find a way to make certain molecules in a very specific shape. They knew that enzymes are very good at helping make molecules in the right shape, but they are not as good at controlling certain reactions. So, the scientists decided to use a specific enzyme called Thiamine diphosphate (ThDP)-dependent lyase to see if they could make molecules in the right shape.

To do this, they used a process called protein engineering, which means they changed the enzyme's structure to make it work better. They also combined it with something called organophotoredox catalysis, which is a fancy way of saying they used light to help the enzyme do its job.

The enzyme they used makes something called ketyl radicals, which are special molecules that can react with other molecules to make new ones. The scientists used a special dye that, when it gets excited by light, can give the enzyme the energy it needs to make these ketyl radicals. Then, the enzyme can react with other molecules to make new molecules in a specific shape.

They tested this method with many different molecules, and they were able to make them in the right shape with very high accuracy. They even figured out how this process works by studying it in detail.

This study is important because it shows that enzymes can be used in a new way to make molecules in a specific shape. It also gives scientists a new tool to control certain reactions and make molecules that can be useful in many different ways.

Xu Y., Chen H., Yu L., Peng X., Zhang J., Xing Z., Bao Y., Liu A., Zhao Y., Tian C., Liang Y., Huang X. A light-driven enzymatic enantioselective radical acylation. Nature. 2024 Jan;625(7993):74-78. doi: 10.1038/s41586-023-06822-x. Epub 2023 Dec 18.