Semiempirical method for examining asynchronicity in metal-oxido-mediated C-H bond activation.

ABSTRACT: The oxidation of substrates via the cleavage of thermodynamically strong C-H bonds is an essential part of mammalian metabolism. These reactions are predominantly carried out by enzymes that produce high-valent metal-oxido species, which are directly responsible for cleaving the C-H bonds. While much is known about the identity of these transient intermediates, the mechanistic factors that enable metal-oxido species to accomplish such difficult reactions are still incomplete. For synthetic metal-oxido species, C-H bond cleavage is often mechanistically described as synchronous, proton-coupled electron transfer (PCET). However, data have emerged that suggest that the basicity of the M-oxido unit is the key determinant in achieving enzymatic function, thus requiring alternative mechanisms wh

SUBMITTER: Barman SK 

PROVIDER: S-EPMC8433561 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature