Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.

ABSTRACT: Manganese cofactors activate strong chemical bonds in many essential enzymes. Yet very few manganese-dependent enzymes are known to functionalize ubiquitous carbon-hydrogen (C-H) bonds, and those that catalyze this important reaction display limited intrinsic reactivity. Herein, we report that the 2-aminoisobutyric acid hydroxylase from Rhodococcus wratislaviensis requires manganese to functionalize a C-H bond possessing a bond dissociation enthalpy (BDE) exceeding 100 kcal/mol. Structural and spectroscopic studies of this enzyme reveal a redox-active, heterobimetallic manganese-iron active site that utilizes a manganese ion at the locus for O ₂ activation and substrate coordination. Accordingly, this enzyme represents the first documented Mn-dependent monooxygenase in bi

SUBMITTER: Powell MM 

PROVIDER: S-EPMC10029006 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature