How to Stabilize Carbenes in Enzyme Active Sites without Metal Ions.

ABSTRACT: Carbenes are highly reactive compounds with unique value to synthetic chemistry. However, a small number of natural enzymes have been shown to utilize carbene chemistry, and artificial enzymes engineered with directed evolution required transition metal ions to stabilize the carbene intermediates. To facilitate the design of broader classes of enzymes that can take advantage of the rich carbene chemistry, it is thus important to better understand how to stabilize carbene species in enzyme active sites without metal ions. Motivated by our recent studies of the anaerobic ergothioneine biosynthesis enzyme EanB, we examine carbene-protein interaction with both cluster models and QM/MM simulations. The cluster calculations find that an N-heterocyclic carbene interacts strongly with polar and po

SUBMITTER: Lai R 

PROVIDER: S-EPMC9671863 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature