References: Structure–function relationships of radical SAM enzymes | Nature catalysis
The so-called radical S-adenosyl-L-methionine (SAM) proteins belong to a large family of catalysts. These catalysts use the electron reduction of an Fe-S metallic center to produce a highly reactive 5’-deoxyadenosyl radical species which can then initiate a wide variety of radical reactions on a variety of different substrates including small organic molecules, proteins, DNA and RNA. Because they catalyze very complex reactions, these enzymes hold promise for a wide array of potential biotechnological uses.
However, the involvement of high-energy intermediate species requires the tight control of this chemistry by the protein matrix. It is therefore essential to understand how this control is achieved in order to develop catalysts as tools for chemical synthesis. This review presents some of the latest developments in the study of these enzymes by focusing on the structure-function relationships of a few examples for which structural, functional and spectroscopic data as well as theoretical calculations are available. This will help to better describe the close interaction between the chemistry performed and the control exerted by the protein matrix.
Part of this work was funded by the DRF-impulsion program.