Non-Aufbau electronic structure in radical enzymes and control of the highly reactive intermediates.

ABSTRACT: Radicals are highly reactive, short-lived chemical species that normally react indiscriminately with biological materials, and yet, nature has evolved thousands of enzymes that employ radicals to catalyze thermodynamically challenging chemistry. How these enzymes harness highly reactive radical intermediates to steer the catalysis to the correct outcome is a topic of intense investigation. Here, the results of detailed QM/MM calculations on archetype radical B₁₂-enzymes are presented that provide new insights into how these enzymes control the reactivity of radicals within their active sites. The catalytic cycle in B₁₂-enzymes is initiated through the formation of the 5'-deoxyadenosyl (Ado˙) moiety, a primary carbon-centred radical, which must migrate up to 8 Å to rea

SUBMITTER: Khalilian MH 

PROVIDER: S-EPMC11290419 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature